Bl2

VOLUME 1 Chemistry

Edited by DAVID DOLPHIN Department of Chemistry University of British Columbia

1807 ML/1982

A WILEY-INTERSCIENCE PUBLICATION JOHN WILEY & SONS New York • Chichester • Brisbane • Toronto • Singapore

Contents

1 History of Vitamin B12: Pernicious Anemia to Crystalline Cyanocobalamin 1 Karl Folkers

1 100 to 155 Years Ago, 1 2 56 to 100 Years Ago, 2 3 53 Years Ago—The Nobel Prize, 2 4 36 to 53 Years Ago, 3

5 32 Years Ago-Discovery of Crystalline Vitamin B12, 3 References, 15

2 Nomenclature 17

Waldo E. Cohn

3 X-Ray Crystallography of B12 and Cobaloximes 23

Jenny Pickworth Glusker

1 Establishment of the Chemical Formula of Vitamin BI2 and Vitamin Bi2 Coenzyme 24

2 Details of the Structure of Vitamin B12, the Coenzyme, and Their Analogues, 41 3 Effects of Alterations in the Corrinoid System, 69 4 Model Compounds to Give Information on Mechanism, 80 5 Concluding Remarks, 90 Notes Added in Proof, 91 Appendix I Lists of Analyses Described, 92 Appendix II Methods of X-Ray Crystallography and Glossary, 97 References, 102

4 Biosynthesis of the Corrin Macrocycle 107

Alan R. Battersby and Edward McDonald

1 Introduction, 108 2 Identity of the Primary Precursors of Cobyrinic Acid, 111

3 Mechanistic Study of the Methyl Transfer from Methionine, 113 4 Proof That Uro'gen-III Is a Precursor of Cobyrinic Acid, 116 5 Biosynthesis of Uro'gen-III from PBG ,117 6 Steps Beyond Uro'gen-III ,120 7 Structures of the Dimethylated Isobacteriochlorins

Related to Vitamin B12, 123 8 Structure of the Mono-C-Methylated Chlorin (Factor I), 130 9 Structures of the Trimethylated Isobacteriochlorins, 132

10 The Methyltransferase Enzyme System, 135 11 Synthesis of Isobacteriochlorins and Dihydroisobacteriochlorins, 135 12 Experiments on the Loss of C-20 from the Precursor Macrocycle During Formation of Cobyrinic Acid, 137 13 Summary of Pathway to Corrins and Future Prospects, 139 References, 141

Biosynthesis of Cobalamin Coenzymes 145

F. M. Huennekens, K. S. Vitols, K. Fujii and D. W. Jacobsen 1 Introduction, 146 2 Biosynthesis of the Nucleotide Loop of Cobalamins: Conversion of Cobyric Acid to Cobalamin, 148 3 Formation of the Car bon—Cobalt Bon d in C obalamin Co enzymes: Conversion of Cob alamins to Ade nosyl- and Meth ylcobalamin, 15 5 References, 164

The Total Synthesis of Vitamin B12 169

Robert V. Stevens

1 Introduction, 169 2 Synthesis of Cyanobromide 1 (Harvard, 1968), 172 3 The Eastern Half (Cambridge and Zurich), 183 4 Coupling of th e Eastern a nd W estern Halves: S ynthesis of Cob yric Ac id (Cambridge and Zurich), 187 5 The Photochemical Path (Zurich), 192 6 Synthesis of Vitamin B12, 197

Reactions of the Corrin Macrocycle 201

Raymond Bonnett

1 Introduction, 202 2 The Corrin Ligand-Basic Structural Considerations, 203 3 Metallation and Demetallation, 210 4 Meso Substitution, 212 5 Oxidative Cleavage, 217 6 Epimerization at 0-Positions, 220 7 Cyclization Reactions, 225 8 Reactions of Peripheral Acylamide Functions, 230 9 Miscellaneous Reactions, 237 References, 240

7 Synthesis of Organocobalt Complexes 245

Kenneth L. Brown

1 Introduction and Scope of This Chapter, 246 2 Practical Aspects, 247 3 Organocobalt Syntheses via Cobalt (I) Reagents, 250 4 Organocobalt Syntheses via Cobalt(II) Reagents, 271 5 Organocobalt Syntheses via Cobalt(III) Reagents, 277 6 Modification of Organic Ligands, 283 References, 286

9 Reactions of Alkyl Ligands Coordinated to Cobalamins and Cobaloximes 29 H. P. C. Hogenkamp

1 Introduction, 295 2 Homolytic Cleavage of the Carbon—Cobalt Bond, 296 3 Heterolytic Cleavage of the Carbon—Cobalt Bond, 305 References, 319

10 Coordination Chemistry of the B12 Dependent Isomerase Reactions 32 J. M. Pratt

1 Introduction, 326 2 Why Co? 335 3 Steric Effects on the Structures and Equilibria of DBC and Alkylcobalamins, 341 4 Labilization of the Co—C Bond by Steric Distortion, 361 5 Reactions Related to the Enzymatic Isomerase Reactions, 375 6 Summary, 386 References, 388

11 Electronic Spectra of B12 and Related Systems 393 C. Giannotti 1 General Aspects in the Electronic Transition of Corrinoid Co111 Compounds, 394 2 Theoretical Considerations, 396 3 Nature of the Electronic Transitions, 401 4 Effect of Various Parameters on the Position of the Absorption Bands, 407

5 Electronic Absorption Spectra of B12r and B12s, 418 6 Cobaloximes as Models, 419 7 Circular Dichroism (CD); Magnetic Circular Dichroism (MCD), 420 8 Luminescence, 426 References, 427

10 EPR of B12-Dependent Enzyme Reactions and Related Systems

John R. Pilbrow 1 Introduction, 432 2 EPR of Cobalamins and Cobinamides, 433

3 B12 -Dependent Enzyme Reactions, 444

4 Oxygenation of B 12r(Cbl"), 458 5 Conclusion, 459 References, 460

13 The Nuclear Magnetic Resonance Spectroscopy of Cobalamins and Their Derivatives 463 Otto D. Hensens, H. Allen O. Hill, Charlotte E. McClelland, and Robert J. P. Williams

1 Introduction, 464 2 The 1H NMR Spectrum of Adenosylcobalamin, 465 13 3 C NMR Assignments of Vitamin B12 Derivatives, 473 4 Structural Information Revealed by NMR Spectroscopy, 482 5 Biosynthetic Studies, 486 6 The 1H NMR Spectra of Co (II) and Co (I) Corrinoids, 486 7 The Electronic Structure of Corrinoids, 487 8 The Cobalamins as Fluxional Molecules, 490 9 The pH Dependence of the 1H NMR Spectra of Cobalamins, 493

10 The Reaction of Cobalamins with Metal Ions, 495 11 Conclusions, 498 References, 498

11 Chemistry and Significance of Vitamin B12 Model Systems 501

Jack Halpern

1 Introduction, 502

2 Some General Comparisons of B12 and Model Compounds, 504 3 Structural and Steric Aspects, 505 4 Acidities of Hydridocobalt Complexes and Cobalt—Hydrogen Bond Dissociation Energies, 506 5 Cobalt—Carbon Bond Dissociation Energies, 507

6 Redox Chemistry of BJ2 Model Compounds, 513 7 Formation of Cobalt—Carbon Bonds, 517 8 Cleavage of Cobalt—Carbon Bonds, 524 9 Role of Model Systems in the Study of the Mechanisms

of B12-Dependent Enzymatic Reactions, 528 10 Concluding Remarks, 535 References, 535

15 Mechanisms of Action of the B12 Coenzyme: Theory and Models 543

Bernard T. Golding

1 Introduction, 544 2 Cleavage of the Co—C Bond of AdoCbl, 544 3 Hydrogen Abstraction, 554 4 Migration of Group X, 555 5 Modeling AdoCbl-Dependent Reactions, 564 6 Conclusions, 577 References, 578

CONTENTS OF VOLUME 2

1 Biological and Medical Aspects of Vitamin B12 William S. Beck

2 Cobalamin Transport in Microorganisms

Clive Bradbeer

3 Instrinsic Factor, Transcobalamin, and Haptocorrin

Ebba Nexǿ and Henrik Olesen

4 Quantitation of Cobalamins in Human Serum Ebba Nexǿ Henrik Olesen

5 Metal-Free Corrinoids and Metal Insertion Volker B. Koppenhagen

6 Mechanisms for B12 -Dependent Methyl Transfer J. M. Wood

7 Acetate Biosynthesis Lars G. Ljungdahl and Harland G. Wood

8 Amino Mutases John J. Baker and Thressa C. Stadtman

9 Diol Dehydrase Tetsuo Toraya and Saburo Fukui

10 Ethanolaminc Ammonia-Lyase

Bernard M. Babior

11 Glutamate Mutase

Robert L. Switzer

12 B12 -Dependent Methionine Biosynthesis Robert T. Taylor

13 Methylmalonyl-CoA Mutase

Jdnos Retey

14 Cobalamin-Dependent Ribonucleotide Reductases

Raymond L. Blakley Preface for Volume 1

Volume 1 contain s chapters on the history, nomenclature, and structure determina- tions of B12 and related systems. The biosynthesis of the corrin macrocycle and co- enzyme B are covered , along with th e total chemical synthesis of the vitamin. 12 Reactions o f both the corrin ring and the cobalt-carbon bond are discussed and related to the mechanism of action of coenzyme B12. In addition, chapters on vari- ous aspects of spectroscopy including electronic, EPR, and NMR are included. The final result is an up-to-date and critical review of the areas described above. This treatise provides, for the first time, a complete and comprehensive review of all of the major chemical, biochemical, and medical aspects of vitamin B12. I wish to tak e thi s opportunity to thank the contributors t o thi s volume for both the scholarshi p of their work and the promptness with which they all met the various deadlines.

DAVID DOLPHIN

Vancouver, British Columbia November 1981

General Preface

The vitami n B12 coenzyme and related corrinoids represent the most complex non- polymeric structures found i n nature , and in addition they are the only known nat- urally occurring organometallic complexes. Their uniqueness and complexity have presented majo r challenges, and will continue so to do for some time to come, in all areas o f the natural and life sciences . Indeed, solutions to B12-related problems pre- sent some of the principal scientific achievements of the past half century; each decade has recorded a milestone toward s an understanding of the nature and func- tion o f these systems . In 1926 Minot an d Murphy announced a dietary treatment of pernicious ane - mia, which had previously proved t o be a fatal disease. In 1934 they were awarded the Nobel Prize for their discoveries concerning liver therapy against anemias . I n 1948 Folker' s group i n th e United States and Leste r Smith's in Great Britain inde- pendently announced the isolation and crystallization of the red antipernicious ane- mia factor now known as vitamin B12. The structure of vitamin B!2 wa s revealed in 1956 by th e X-ray crystallographi c work o f Hodgkin's group an d by the chemical studies o f Todd an d Johnson . I n 1958 Barker isolated and characterized coenzyme

B12, showing that vitami n B12 (cyanocobalamin ) is an antifact generated during its isolation. The structure of the coenzym e with its unique cobalt-carbon bond wa s elucidated once mor e b y Hodgkin i n 1961 . The 1960s saw majo r advance s in our understanding o f both the chemistry and enzymology of B12 and it s coenzyme , culminating in th e total synthesis of vitamin B12 by Woodward and Eschenmoser in 1976.

Since there are fewer molecule s o f B12 i n a man than there ar e red blood cells, it is not surprisin g that there is still much to learn about this molecule. This is espe- cially true in mammal s where the function of Bt2 i n such low concentrations is still unclear. Furthermore , although there are many enzymatic reactions dependent on coenzyme B12, its mechanism of action is still obscure. This wor k consists of two volumes and cover s al l o f th e major aspect s o f the chemistry, biochemistry, and medicine relating to BJ2. Volume 1 emphasizes chem- istry, biosynthesis , history, and nomenclature ; Volume 2 cover s biochemical an d medical aspects . I wish to thank Dr. Olga Avramovic fo r her assistance, Alan Johnson for intro-

ducing me to B12, and the late R. B. Woodward for expanding and encouraging my knowledge an d interest in th e subject .

DAVID DOLPHIN

Vancouver, British Columbia November 1981

Author Index

Numbers in boldface are pages on which names/references appear in text. Numbers in parentheses are reference numbers and indicate that the author's work is referred to although his name may not be mentioned in the text. Numbers in italics indicate pages

on which complete references are listed.

Aasa, R., 437(11), 461 Anh, N. T , 398(15), 400(15), 411(15), Abbott, J. C, 252(41), 288, 418(88), 419(15), 427, 556(38), 562(38), 564 419(88), 430 (38), 576(38), 579 Abeles, R. H., 65(56), 68(57), 104, 109 Anton, D. L., 313(76), 322 (1), 141, 147(11), 156(52), 160(52), Anton, P. L., 486(36), 499 164, 166, 282(188), 283(188), 284 Arigoni, D., 115(17, 20, 22), 116(20), (188), 239, 310(64), 322, 376(93), 126(55), 132(55, 59, 70), 142,144, 377(95), 382(121, 122), 391, 392, 377(96), 391, 545(4), 558(4, 46), 577 449(27, 30), 450(41), 451(36, 37, 41), (4), 578, 580 453(41), 454(41), 461, 462, 469(14), Armarego, W. L. F., 277(172), 292 499, 507(31), 527(118,119), 530(31), Armitage, I. A., 115(19), 117(26), 120 536, 539, 540, 545(5, 27), 547(6, 16), (26), 133(19), 142 548(11, 16), 550(11, 16), 551(17), 558 Armitage, J. B., 230(79), 234(79) (47), 559(47), 578, 579, 580 Ash, L. B., 33(33), 103 Abley, P., 255(80), 278(80), 289, 526 Ashcroft,M. R., 381(118), 392, 568(63), (107), 527(107), 538, 539 569(63), 570(63), 580 Ackermann, G., 404(26), 427 Assour, J. M., 438(15), 461{\5) Adams, W. W., 85(88), 87(88), 88(88), Atkins, M. P., 268(125), 291, 381(116), 105 392, 568(64, 65, 66), 569(64, 65, Adamson, A. W., 406(52), 428 66), 570(65), 580 Adin, A., 526(106), 539 Auh, N. T., 530(131), 540 Agnes, G., 311(69), 312(69), 322, 527 Awtrey, A., 352(65), 390 (110, 112), 539 Awtrey, A. W., 244(18, 19), 249(18), 271 Ahond, A., 256(74), 264(74), 304(42), (18), 283(18), 287 321, 364(83), 391, 404(37), 405(37), 418(31), 428, 511(49), 537 Babior, B. M., 109(1), 141, 147(9), 155 Alcock,N. W., 706(118) ( 9 ) , 164, 254(66), 289, 282(194), 291, Alicino, J. F., 26(10), 102 293, 331(8), 332(8), 367(8), 376(94), Allen, R. H., 268(121), 291 381(120), 388, 391, 392, 423(102), Allerhand, A., 473(18), 480(18), 481 430, 449(28, 32), 450(32), 451(28, 32), (18), 484(30), 491(18), 499 452(46), 453(32), 457(46), 461, 462, Allingcr, J., 33(33), 33 469(15), 499, 507(30), 529(126), 530 Alworth, W. L., 110(3), 120(3), 141 (30, 126), 534(126), 536, 540, 541, Anderson, B. F., 75(68), 105 544(la), 555(34), 558(46, 49), 575(82, Anderson, S. N., 269(136), 291, 516 83), 576(92), 578, 579, 580, 581, 582 (74), 538 Bachovchin, W. W., 554(30), 555(30), 579

Bacquet, R., 352(65), 390 Beck, W. S., 160(65), 166 Bacquet, R. J., 271(148), 292 Becker, W., 37(43, 44), 39(43), 40(47) Bailey, N. A., 279( 175), 292, 336(25), 104, 229(74), 230(78), 242 389 Beckham, T. M., 262(103), 263(102), Baker, H. N., 110(3), 120(3), 141 290, 363(82), 391, 571(70), 581 Ballard, D. H., 269(136), 291, 516(74), Beckhans, H-D., 548(10), 578 538 Beinert,H., 381(120), 392, 449(32), 450 Baltimore, B. G., 449(31), 461, 571(69), (32, 35), 451(32), 453(32), 455(35, 53) 581 456(53), 461, 462, 558(49, 50), 580 Balzani, V., 406(50), 428 Beisbarth, H., 231(84), 242 Banks, A. R., 575(87), 581 Belford, R. L., 440(23, 24), 461 Banks, R. G. S., 335(14), 373(90), 389, Belikov, A. B., 298(12), 299(12), 320, 391 363(81), 391, 573(77), 557 Bannister, J. V., 468(13), 499 Bendle,S., 527(112), 539 Bannister, W. H., 468(13), 499 Bercaw, J. E., 515(65), 537 Bansal, K. M., 573(76), 581 Bergmann, K.-H., 123(47, 48), 125(47, Barchielli, R., 152(26), 154(26), 165 48), 126(47), 127(47), 128(47), 13o' Barker, H. A., 30(31), 54(53), 103,104, (47), 132(48), 134(48), 143 147(1, 2), 152(27), 156(43,47), 159 Bernhauer, K., 110(2), 120(2), 747, 148 (43), 164, 165, 296(2), 297(3), 305(44), (14), 151(21), 152(24, 28), 164,165, 306(52), 312(72, 73), 319, 320, 321, 312(71), 316(87), 322, 323, 417(79), 322, 331(9, 10), 353(68), 366(10), 429, 216(46), 221(63), 226(46), 230 367(91), 388, 390, 418(92), 430, 449 (81, 82), 231(83, 84, 89), 235(91), (31), 452(45), 457(45), 461, 462, 571 236(94, 95), 238(82), 241, 242, 243, (69), 581 254(67), 278(174), 289, 292 Barnett, R., 310(64), 322, 527(118, 119), Bertele,E., 236(96), 243 539 Bidling,G., 87(125), 106 Barrick, J. C, 85(92), 705 Bidlingmaier, G., 377(101), 392, 533 Bartczak, T. J., 75(68), 105 (146, 147, 148), 540, 564(54), 580 Bartels,G., 219(58), 242 Bieganowski, B. R., 413(72, 73, 74, 75, Bartlett, M. W., 75(65), 87(100), 88(100), 76), 415(72), 420(72, 73), 421(72, 73), 104, 105, 269(138), 291 429 Bartosinki, B., 165(41) Bieganowski, R., 92(127), 106 Battaglia, L. P., 706(110) Bigotto, A., 106(107), 256(91), 270(91), Battersby, A. R., 111(8), 112(14), 113 280(91), 290, 336(24), 389, 391, 502 (14), 114(18), 115(18), 116(8, 25), (3), 505(17), 514(3), 531(17), 535, 536 117(25, 28,29,31), 118(28, 29, 33, Birke, R. L., 514(60), 522(60), 537 35, 36, 37), 120(25b), 121(41), 122 Blach, D. STC, 92(128), 106 (43, 46), 123(43, 46, 49), 125(43, 46, Blackburn, R., 318(94, 96, 97), 319(97), 51), 126(46,51,53), 127(28a), 128 323, 376(91,92), 391 (46), 129(43,56), 130(56), 132(49, Blackmer, G. L., 258(96), 290 60), 133(60, 61), 134(61), 135(43, 60, Blakley, R. L., 313(74), 322, 432(2, 3), 61, 64, 66), 137(61), 141(69), 142, 143, 433(2, 3), 439(3), 441(3), 442(3), 449 144, 218(56), 242, 482(25), 486(37), (3, 34, 39), 450(35), 451(39, 40), 453 499, 500 (39, 40), 455(35, 52, 53, 54, 55), 456 Batton, P., 281(185), 293 (52, 53, 54), 460, 461, 462, 558(50), Bayston, J., 458(56), 462 580 Bayston, J. H., 439(21), 442(21), 443 Blandhard, H. S., 404(23), 427 (21), 444(21), 445(21), 449(21), 461 Barker, H. A., 432(1), 460 Bayston, J. N., 277(167), 292 Blaser,H., 273(158), 292 Beavan, G. H., 204(8), 215(8), 240 Blaser, H. U., 211(32), 241, 513(59), Beaven,G. H., 41S(9\),430 520(59), 522(59), 535(59), 537 Beavin, G. H., 277(165), 292 Blaylock,B. A., 162(72), 166

Boas, J. F., 381(119), 382(119), 392, Brodie, J. D., 163(78), 166, 255(87), 289, 438(12a), 452(44), 453(44), 454(44), 306(53), 321, 343(58), 344(58), 349(58), 457(44), 461, 462, 559(51), 580 350(58), 354(58), 362(76), 369(76), 390, Bock, D. L., 260(99), 290 391, 426(106), 430, 469(16), 471(17), Bogard, T. L., 118(38), 126(54), 143, 486(17), 487(17), 499 144 Brot, N., 163(79, 84), 167, 254(71), Bolton, J. R., 404(38), 405(38), 418 289 (38), 428, 525(94, 95), 538, 539 Brown, C. E., 112(12), 142 Bonneau, R., 404(42), 418(42), 419(42), Brown, D. G., 291(119), 307(59), 322, 428 430, 432(4), 449(4), 460, 469(15), 486 Bonnett, R., 33(39), 103, 110(5), 120 (35), 499, 504(7, 10), 528(7, 10), 535, (5), 125(50), 141,143, 153(30), 165, 536 202(2, 4), 203(4), 204(2), 208(24), Brown, D. L. S., 508(40), 537 212(12), 215(2, 11), 218(2), 220(2, Brown, K. L., 248(14, 17, 20, 21, 22), 11), 221(62), 222(64), 224(24, 64), 249(14, 17, 18), 254(72), 256(89), 225(11), 226(11), 227(11), 229(75), 257(89), 266(89), 270(145), 271(18, 230(87), 231(87), 233(87), 234(4, 62, 148), 276(145), 278(173), 283(18, 22), 65, 80), 235(62), 236(11, 65), 238(11), 284(17), 287, 289, 292, 302(33), 308 240, 241, 242, 345(60), 390, 417(81), (60, 61, 62), 309(60), 311(67), 314 418(80), 429, 485(33), 499 (11), 321, 322, 352(65), 390, 504(13), Boos, R. N., 419(94), 430 527(117), 529(117), 534(1?5), 536, Boretti, G., 152(26), 154(26), 165 539, 575(86, 89), 581, 582 Borodulina-Shvets, V. I., 267(109), 290 Brown, T. L., 494(49), 496(49), 500 Borodulino-Shvets, V. I., 305(49), 306 Brownson, C, 449(34), 461 (49), 321 Bruckner, S., 706(106), 343(51), 349(51), Boucly, P., 251(39), 288 360(51), 390, 505(16), 531(16), 536 Boudy, P., 279(179), 293 Brydon, G. A., 514(60), 522(60), 537 Bovmann, D., 212(36), 220(36), 241, Buchanan, D. H., 254(75), 260(98), 268 345(61), 390 (138), 289, 290, 291, 317(88), 323, Bowden, F. L., 329(5), 345(5), 388 523(88), 538 Bower, B. K., 125(50), 144 Buchler, J. W., 125(50), 144 Bowman, J. T., 249(25), 254(24), 278 Buckel, W., 115(21), 142 (25), 287 Buckman, T., 297(120), 303(36), 321, 405 Bowman, R. L., 426(106), 430 (45), 428 Boxer, G. E., 404(43), 428 Bud6-Zahonyi, E., 248(23), 252(23, 47, Boyle, M. F., 514(60), 522(60), 537 50), 253(47, 60, 61), 288 Bozdech, J. ML, 455(52), 456(52), 462 Buettner, G. R., 382(123), 386(124), 392, Brady, R. O., 156(43), 159(43), 165, 418 451(43), 452(43), 453(43), 454(43), {92),430 457(43), 462 Bragg, W. L., 24(2), 102 Buhler, N., 239(102), 243 Braterman, P. S., 340(41), 389 Buisson, D. H., 468(12), 499 Bray,R.C, 111(10), 142, 218(51), 241, Bukin, V., 121(42), 122(42, 43), 125 486(39), 500 (45), 129(43), 135(43), 143 Bresciani-Pahor, N., 86(95, 111), 87(112), Buley, A. L., 532(135), 534(135), 540 105,106, 359(72), 375(72), 382(72), Bunn,C. W., 106(122) 391, 491(47), 500, 505(18, 19, 20), 506 Burgi, H. B., 398(15), 400(15), 411(15), (20), 531(18, 19, 20), 536 419(15), 427, 530(13), 540, 556(38), Breslow, R., 261(102), 290, 379(108), 392 562(38), 564(38), 576(38), 579 Briat, B., 418(86), 426(86, 103), 429, 430 Burke, G. T., 163(78), 766 Brink, C, 26(11), 102 Burnett, M. G., 252(49), 288 Burnham, B. F., 479(22), 484(22), 487 Brink, N. G., 25(5), 102, 239(104), 243 (22), 499 Brink-Shoemaker, C, 26(19), 103, 342 Burton, G., 118(34), 143 (43), 389

Bury, A., 381(118), 392, 568(63, 66), Charton, M., 256(85), 271(85), 289 569(63, 66, 67) , 570(63), 580, 581 Chaston, S. H. H., 438(12b), 461 Busch, D. H., 250(33, 34), 287, 288, Chatt, J , 340(39), 389 404(35), 418(35), 42* Cheh, A., 539 Bushell, M. J., 144(11) Chemaly,S., 567(61), 580 Bykhovsky, V., 122(43), 123(43), 125 Chemaly, S. M. , 343 (54), 344(54), 351 (43), 129(43), 135(43), 143 (54), 352(54), 353(54), 355(54), 357 Bykhovsky, V. Ya., 121(42), 122(42), (54), 358(54), 359(54), 360(54), 362 125(51), 126(51), 143, 144 (54, 78) , 364(54), 365(54, 86) , 366 (54), 368(54), 371(54), 376(54), 379 Cacevar,C, 526(109), 539 (78), 380(86), 390, 391 Cagen, L. M., 157(58), 166 Cheney, B. V., 130(58), 144 Calderazzo, F., 254(64), 289, 335(20), Chernoff, D., 248(21), 287 389 Chervyakova, T. G., 282(189, 190), 284 Calligaris,M., 86(95, 111), 87(112), 105, (199, 201, 202, 203), 285(202), 293, 106, 343(51), 349(51), 359(72), 360 294, 549(14), 575(85), 578, 581 (51), 375(72), 382(72), 390, 391, 491 Cheung, A., 469(14), 499 (47), 500, 505(16, 18, 19), 531(16, 18, Chin, C. A., 422(101), 426(101), 430 19), 536 Chock, P. B., 273(155), 292, 352(65), Callot, H. J., 280(183, 184), 281(183, 390, 511(48), 518(48), 519(48), 535 184), 293 (48), 537 Cambridge group, 135(65), 144 Chrzastowski, I. Z., 516(74), 538 Candlin, J.?., 428 Chrzastowski, J. Z., 525(100), 526(100), Cannon, A. W., 230(79), 234(79, 80), 539 242 Chu,M. M. L., 575(89), 582 Cannon, J., 27 Chung, S. K., 379( 107), 392, 532( 145),540 Cannon, J. R., 110(5), 120(5), 141, 202 Cioffari, A., 556(44), 580 (2), 204(2, 11), 215(2, 11), 218(2, 50), Clark, V. M„ 110 (5), 120(5), 141, 204 220(2, 11), 225(11), 226(11), 227(11), (11), 215(11), 218(55), 220(11, 55) , 231(11), 236(11), 238(11), 240, 241, 225(11), 226(11), 227(11), 231(11), 417(81), 418(80), 429 236(11), 240, 242, 418(80), 429 Cantoni,G. L., 156(46), 165 Clarke, D. A ., 246(3), 252(3), 266(3), Carassiti, V., 406(50), 428 277(3), 286, 302(32), 321, 335(19), Cardin, D. J., 299(13), 320 389 Carr, J. E., 419(94), 430 Clauser,S. C, 412(66), 429 Carr, S.G., 453(50), 462 Cocevar,C, 525(99), 539 Carrell,H. L., 24(1), 102, 106 Cockle, S. A., 353(66, 67), 390, 430, Carry, T. J., 282(188), 283(188), 284 439(206), 451(38), 452(38), 456(6), (188), 293 458(57), 461, 462, 468(11), 469(11), Cason,J.,33(33),70J 498, 499, 558(48), 580 Cass, A. E. G., 468(13), 499 Coffman, R. E., 382(123), 386(124), Castanera, E. G., 156(43), 159(43), 165 392, 451(40, 43), 452(43), 453(43), Castro, C. E., 522(86), 538 454(43), 455(53, 54), 456(53, 54), Caughlin, C. N., 404(25), 427 457(43), 462 Cesari,M., 280(182), 293 Coleman, W. M., 252(40), 288 Chan, M. S., 515(70), 516(70), 535(70), Collar, J. W., 252(41), 254(41), 288, 418 538 (88), 419(88), Chanser, E. G., 298(8), 320, 363(80), Conn, J. B., 419(94), 430 391 Connolly, P. J., 252(49), 288 Chao, T.-H., 252(45), 253(59), 269(135), Connor, J. A., 508(40), 537 288, 291, 507(27), 536 Cooksey, C. J., 266(108), 267(108), 285 Charbonneau, L., 490(50), 495(50), 497 (205), 286(205), 290, 294, 525(100), (50), 500 526(100), 539, 569(67), 581

Cooper, N. J. , 5 30(132), 540, 547(8), Davis, J. A., 92(128), 106 559(8), 576(8), 578 Day, P., 396(5, 6), 397(5, 6), 398(5, 6), Cooper, N. John, 452(49), 462 401(5), 403(5), 409(5, 6), 427, 487 Corcoran, J. W., 111(9), 142 (41), 500 Corey, E. J. , 45 2(49), 462, 530(132), DeBolfo, J. A., 462(59) 540, 547(8), 559(8), 576(8), 578 Deeg, R., 123(47, 48), 125(47, 48), 126 Cornforth, J. W., 115(21), 142 (47), 127(47), 128(47), 129(57), 130 Corradi, A. B., 706(110) (47), 132(48, 57, 59), 134(48, 57), Costa, G., 250(35), 254(63, 65), 256 135(57), 137(57), 143, 144 (91), 270(91, 143), 271(143, 146), Demon, P., 115(19), 133(19), 142 277(170, 171), 280(91), 288, 289, 290, Deniau, J., 512(56), 525(56), 537 291, 292, 301(28), 317(90), 320, 323, Deppish,B., 87(125), 106 336(24), 389, 490(45), 500, 502(3, 4), Derynck, J., 251(39), 279(179), 288, 504(4), 514(3, 4, 61, 62, 63), 525(99), 293 526(109), 535, 537,539 deSavorgnani, E., 271(146), 292 Coulter, C. L., 35(48), 103, 154(36), 165, DeSimone, R. E., 490(50), 495(50), 497 342(45), 389 (50), 500 Cox, D. L., 318(94), 323 Deutsch, E., 85(91, 94), 105, 158(61), Craig, P. J., 330(6), 335(6), 338(30), 166, 250(30, 31), 253(30), 254(31), 349(6), 361(6), 364(6), 366(6), 367(6), 258(31), 287, 391 388, 389, 419(97), 430, 504(9), 508 Devaquet, A., 398(15), 400(15), 411(15), (9), 536 419(15), 427, 556(38), 562(38), 564 Cram, D. J., 547(9), 548(9), 578 (38), 576(38), 579 Crosby, G. A., 406(57), 428 De Vries, B., 507(26), 536 Cross, R.J.,340(41), 389 Dewar, M. J. S., 567(60), 580 Crowfoot-Hodgkin, D., 75(66), 104 Dicker, I. D., 243(100) Cruichshank, D. W. J., 26(19), 103, 342 Diehl, H., 418(87), 430 (43), 389 Diehl, N., 239(103), 243 Crumbliss, A. L., 249( 24, 25) , 2 54(24), DiGirolamo, P. M., 163(82), 167, 300(16) 268( 132, 133), 278(24, 25), 287, 291 320 CuUen, W. R., 575(87), 581 Dilworth, M. J., 529(124, 125), 540 Cummins, D., 279(176,177), 282(177), 293 Dimarco, A., 110(2), 120(2), 141, 152(26 Currie, M., 78(74), 105 154(26), 765 Cushley, R. J ., 112(13), 113( 16), 142, Dimsdale, M. J., 229(75), 242 473(19), 479( 19), 480( 19), 481( 19), Dizikes, L.,559 499 Dizikes, L. J . , 539 Cutler, A. R., 575(87), 581 Djerassi, C, 418(86), 426(86, 103), 429, 430 Dale, D., 33( 36, 37) , 103, 205(15), 207 Doak,G. O., 340(38), 389 (15), 240, 342(47), 344( 47), 3 47(47), Doblcr, M., 77(71), 78(71), 105 390 Dockal, E. R., 255(80), 278(80), 289, Dalling, D. K. , 480(23), 48 1(23), 488 526(107), 527(107), 538, 539 (23), 499 Dodd, D., 246(2), 256(2, 93), 257(93), Dalton, D. , 379( 107), 392, 532( 145) , 261(93), 263(93), 265(93), 266(108), 540 267(108), 268(134), 277(166), 285 Danon, J , 338(35), 389 (204, 205), 286(204, 205), 286, 290, Das, P. K., 252(44), 288 291, 294, 330(7), 335(7), 364(7), 365 Dauner, H.-O., 117(27, 30), 142 (7) , 367(7), 388, 504(8), 516(74), 517 Davaquet, A , 530(131), 540 (8) , 525( 101), 527( 101), 536, 53 8, 539 Davidson, A , 438(16), 461 551(18), 579 Davies, M. T., 352(64), 365(64), 390 Doddrell, D., 473(18), 480(18), 481(18), Davies, S. P., 451(38), 452(38), 462, 558 484(30), 491(18), 499 (48), 580 Dodson, E., 91(126), 106

Dolphin, D., 109(1), 747, 147(11), 764, Eckert, R., 402(21), 403(21), 420(21), 427 216(43, 45), 241, 246(3), 247(11), 248 Ecoles, T. K., 78(77), 105 (15, 16), 249(11), 251(11), 252(3), 254 Edelev, M. G., 282(189), 284(199, 202 (11), 257(11), 266(3), 277(3), 281(15, 203), 285(202), 293, 294, 549(14), 16, 187), 282(15, 16, 187, 188, 194), 575(85), 578, 581 283(187, 188,195, 196, 197), 284(188, Edelhansen, J. H., 404(44), 428 197), 286, 287, 293, 302(29, 32), 306 Edelstein, N., 438(16), 461, 466 (54) , 315( 79, 80, 8 1, 82, 83) , 316( 82, Edmond, E., 33(38, 39), 103, 208(24), 83), 318(54), 321, 322, 323, 376(93), 223(67), 224(24, 67), 241, 242, 342 391, 418(89), 419(89), 429, 430, 449 (46), 345(60), 390 (27), 461, 507(31), 508(34), 524(34), Edmond, E. D., 75(66), 104, 706(120) 530(31), 534(152, 154, 156), 536, 538, 207(20), 240, 342(50), 390 541, 547(16), 548(16), 550(16), 575(87), Eggerer,H., 115(21),742, 532(139,140),540 578, 581 Eisenstein, O., 398(15), 400(15), 411(15) Dove, M. F., 110(3), 120(3), 141 419(15), 427, 530(131), 540, 556(38), ' Dowd, P., 377(98, 99, 100, 103), 379(99), 562(38), 564(38), 576(38), 579 392, 532(142, 143), 540, 564(55), 565 Eisner, U., 125(50), 143 (55) , 566(55), 567(62), 571(68), 580, Elder, L. G., 85(84), 105 581 Elder, R. C, 85(86, 89, 90, 91, 92, 93, 94), Dreos, R., 317(90), 323 102(86), 105 Dresow, B , 37(41), 40(47), 74(41), 104 Elkin,M.,3(l),4(l),75 Drevs, H., 335(18), 5S9 Elliot, D. F., 235(92), 243 Drexhage, K. H., 396(2),398(2),401(2),427 Ellis, B., 26(9), 102, 204(8), 215(8), 240 Dubs, P., 113(15), 142 Ellis, P. E., Jr., 85(93), 105 Duc-Hiep,T„ 335(18), 389 Elroi,H„ 574(81), 581 Duetsch,E , 523(87), 538 Elsenhaus, B., 72(61), 104, 211(30), 247 Duggan, D. F., 426(106), 430 Elson,C. M., 281(185), 293 Dunham, W. R., 382(122), 392, 450(41), Elvoi, H., 292(151) 451 (41), 453(41), 454(41), 462, 558(47), Endicott, J. F., 246(6), 271(6, 149), 272 559(47), 580 (149), 287, 292, 299(14), 300(23), 320, Dunhill, R. H., 438(12a), 461 335(13), 336(23), 363(23, 79), 373(23), Dunitz, J. D., 75(62, 63, 64, 65), 77(71), 376(23, 79), 389, 391, 404(40, 41), 405 78(62, 64, 71, 74, 76), 80(62), 87(100), (40, 41), 418(40, 41), 428, 503(5), 508 88(100), 704, 105, 106, 241, 269(138), (5, 41), 511(46), 524(5), 525(5, 46), 535, 291 537,553(25), 554(28), 579 Dunne, C. P., 247(12), 249(1 2), 251(12), Engel, J., 137(68), 744 254(12), 257(12), 287 Epps, L. A., 85(85), 86(85), 105 Duong, K. N. V., 253(53), 256(53, 74, 92, Erkol, A. Y., 318(96), 323, 376(91), 391 93), 257(53, 92, 93), 260(92), 267(92, Ernst, L., 37(43), 39(43), 104, 218(58, 59), 93), 263(53, 92, 93), 264(74), 265(53, 229(74), 242 93), 288, 289, 290, 300(18), 304(42), Ershova,T. E., 298(12), 299(12), 320, 363 320, 321, 364(83), 391, 404(37), 405 (81), 391,513(11), 581 (37), 418(37), 428, 511(49), 512(54, Eschenmoser, A., 75(75), 78(75), 105, 113 55), 524(90), 525(54, 55), 537, 538 (15), 126(54), 135(66), 136(67),742, 744, Durell, J., 156(46), 765 202(5),204(14),207(14),209(5), 211(22), Dwek, R. A., 464(1), 467(1), 471(1), 212(5, 33, 36), 213(40), 214(5), 217(5), 491(1), 498 220(36), 227(5), 230(5), 236(96), 239 (102), 240, 241, 243, 345(61), 390 Eager, R. G., 449(31), 467, 571(69), 581 Espenson, J. H., 252(45), 253(58, 59), 260 Eaton, D. R., 379(115), 392 (100), 269(135), 272(150), 277(150), Ebnbthcv, A., 204(9), 240 288, 290, 291, 292, 507(27), 525(97, 98), Eckert, H., 255(76), 261(76), 289, 523 526(106), 536, 539, 575(90), 582 ( S I ) , 538 Essenberg, M. K., 449(30), 467, 545(2), 578

Esscnberg, M. R., 377(95), 391 Forster, L. S., 406(53), 428 Evans, H., 33(39), 103, 208(24), 224 Foster, M. A., 451(38), 452(38), 462, 558 (24), 241, 345(60), 390 (48), 580 Foster, T., 573(79), 581 Eagerness, P. E., 118(4), 143 Fox, J. P., 398(11), 427 Fanchiang, Y. T., 517(76), 538 Francia, M. D., 312(70), 322, 539 Fantes,K.H., 25(7), 102 Frey, P. A., 377(95), 391, 449(30), 461, Farmery, K., 250(34), 288 545, 578 Farooq,S., 212(33), 241 Frick, T„ 312(70), 322, 539 Farragi,M., 318(95),323 Friedlina, R. G., 556(42), 580 Fee, J. A., 382( 122), 392, 450(41), 451 Friedman, S., 147(5), 164, 529(124, 125), (36, 41) , 453( 41), 454( 41), 462, 558 540 (47), 559(47), 580 Friedmann, H. C., 110(4), 747, 148(12, 13), Feller, B. A , 40(46), 104 150(17), 151(13, 17), 153(31, 32, 33), Felner, I., 247(39) 154(36, 37,40), 155(40), 157(58), 764, Fendler, J. H., 409(62), 429 765, 766 | Fenton, W. A., 156(55), 157(56), 166 Friedrich, W., 92(127), 106, 110(2), 120 Ferraudi, G. J., 300(23), 320, 336(23), (2), 747, 152(24), 161(71), 765, 766, 363(23), 373(23), 376(23), 389, 404 221(63), 231(85), 236(94, 95), 242, 243, (41), 405(41), 418(41), 428, 511(46), 249(27), 267(116), 257, 290, 301(26, 525(46),537, 553(25), 579 27), 320, 413(72, 73, 74, 75, 76), 415 Finkbeiner, H. L., 404(23), 427 (72), 420(72, 73), 421(72, 73), 429 Finke, R. G., 547(150) Fritz, H. L., 260(100), 290, 539 Finlay, T. H., 68(57), 104, 461(29), Fuendes, R., 268(126), 297, 482(24), 545(5), 578 487(24), 488(24), 489(24), 493(24), Firth, R. A., 255(81), 289, 336(27), 497(24), 499 343(52), 346(52), 347(52), 348(52), Fugate, R D., 422(101), 426(101), 430 349(52), 350(52), 351(52), 354(52), Fuhrer, W., 202(5), 209(5), 210(26), 212 362(52), 369(52), 389, 390, 394(1), (5), 214(5), 217(5), 227(5), 230(5), 395(1), 397(8), 404(28), 407(1), 240, 241 408(8), 409(1, 8), 412(67), 420(1), Fujii, K., 162(75, 76, 77), 163(82), 766, 422( 1), 427, 429, 468( 10), 482(29), 767 484(29), 487(29), 488(29), 490(29), Fujii, Y., 295(181) 491(29), 499 Fukui, S., 253(57), 288, 301(25), 302 Fischli, A., 75(75), 204(14), 207(14), 212 (30), 306(51), 311(65), 320, 321, 322, (36), 220(36), 240, 241(39), 345(61), 508(38), 522(84), 524(38), 525(38), 390, 427 536, 538 Flohr, H., 87(99), 88(99), 705, 269(139), Funabiki, T., 569(67), 581 270(141, 142),297, 377(101), 379 Fung, M.M., 397(9), 427 (104, 106), 392, 533(146, 147, 148), Fyfe,J. A., 153(33), 765 540, 564(54), 565(57), 580 Florian, L. R., 85(90), 105 Gakenheimer, W. C, 40(46), 104 Floriani, C, 254(64), 289, 335(20), Gale, I. A. D., 125(50), 143, 204(13), 389 240 Folkers, K., 25(5), 26(8), 102, 110(6), Galivan, J.H., 162(76), 766 747, 2 18(53), 2 39(104), 2 47, 243 Gams, R. A., 156(54), 766 Fontaine, C., 404(36), 405(36), 406 Garbers, C. F., 247(49) (36), 418(36), 419(36), 428, 512 Gardiner, D. J., 344(55), 390, 398(10), (53, 54, 55), 525(53, 54, 55), 427 537 Garstki,C., 765(34) Fookes, C. J. R., 117(28, 32, 33), 118 Gastaldo, C., 33(33), 703 (28, 33, 35, 3 6, 37) , 127( 28a), 742, 143 Gatford, C., 266(108), 267(108), Ford,S.H.,110(4),747,150(17),151(17),764 290

Gaudemer, A., 251(39), 253(53), 256 Gould, D. C, 449(28), 451(28), 467 (53 74, 92, 93), 257(53, 92, 93), 260 Graf, F., 441(25), 442(25), 467 (92), 261(92, 93), 263(53, 92, 93), 264 Grant, D. M., 130(58), 744, 477(20), 480 (74)', 265(53, 93), 279(179), 288, 289, (23) , 481(23), 488(23), 492(20), 499 290, 293, 300(18), 304(42), 320, 321, Grant, M. E., 268(126), 297, 306(56), 364(83), 391, 404(37), 405(37), 418 522, 482(24), 487(24), 488(24), 489 (37), 428, 511(49), 512(53, 54, 55, 56), (24) , 493(24), 497(24), 499 525(53, 54, 55, 56), 524(90), 537, 538 Grate, J. H., 297(5), 307(5), 320, 351(62) Gaus, P. L., 249(24, 25), 254(24), 268 355(62), 357(62), 358(62), 362(62), 364 (132, 133), 278, 291 (62), 367(62), 368(62), 369(62), 370(62) George, P., 412(66), 429 371(62), 390, 511(50), 557, 552(21), 553 Georgopapadakou, N., 117(26), 120(26), (21),579 142 Gratzel, M., 573(76), 581 Ghambeer, R. K., 449(34), 461 Greaves, M. L., 35(40), 103, 342(45), 389 Giannotti, C, 404(36, 38, 39, 42), Green, M. L. H., 335( 17), 340( 17), 389, 405(36, 38, 39), 406(36), 418 452(49), 462, 530(132), 540,547(8), (36, 38, 39, 42), 419(36, 39, 42), 559(87), 576(8), 578 428, 512(53, 54), 525(53, 54, 94, Griffith, J. S., 438(13), 467 95), 537,538, 539, 553(23), Griffith, W. P., 276(160), 292 579 Grigg, R , 77(70), 105, 203(6), 240, 243, Gibson, J. F., 467(14) 246(3), 252(3), 266(3), 277(3), 286, 302 Gilbert, B.C., 573(75), 557 (32), 527, 335(19), 340(37), 389 Gill, J., 527(38), 524(92), 538 Gross, G., 236(95), 245 Glusker,D. L., 33(33), 103 Gruning, B., 37(43, 45), 39(43), 104, 229 Glusker, J. P , 28(23), 47(51), 103,104, (74, 76, 77), 236(98), 242, 245, 485(31), 706(121), 504(12), 536 499 Gneuss, K. D., 123(48), 125(48), 129(57), Gschwend, H., 236(96), 245 132(48, 57), 133(62), 134(48, 57, 62), Guest, J. R., 147(5), 764, 529(124,125),540 135(57, 62), 13 7(57, 62) , 143,144 Gunter, J. B , 554(30), 555(30), 579 Godfrey, J. M., 33(39), 103, 208(24), Gunter, J. D., 426(105), 430 221(62), 224(24), 234(62, 65), 235 GUnthard, Hs. H., 441(25), 442(25, 26), (62), 236(65), 247, 242, 345(60), 390, 458(60), 459(60), 467, 462 485(33), 499 Gunzer,G., 117(30), 129(57), 132(57), Goedken, V. L., 275(159), 292, 335(21), 134(57), 135(57), 137(57), 742, 744 389 Gupta, R. K., 485(34), 499, 569(67), 581 Goh, L. Y., 515(65), 537 Gurevich, V. M., 305(50), 306(50), 527 Golding, B. T., 112(4), 113(14), 114(146), Guseva, A. S., 267(110), 290, 305(50), 742, 218(56), 242, 268(125), 281(116, 306(50), 527 117), 282(192, 193), 284(192, 198), Gustafson-Potter, K. E., 118(35, 36), 745 297, 292, 293, 303(39), 316(39), 527, Gutschow,C., 115(21), 742 452(47, 48), 462, 482(25), 499, 504(15), 507(32), 508(32, 39), 525(39), 528(32), Halpern, J., 253(54), 255(80), 264(105), 529(32), 530(32), 532(136, 137, 138), 273(152, 153, 154, 155, 156, 157, 158), 534(136, 149), 556, 557, 540, 549 275(156, 157), 278(80), 288, 289, 290, (If, 14), 547, 553(24), 556(36), 557(36), 292, 335(16), 377(97), 385(97), 389, 558(le, 36), 559(36), 568(64, 65, 66), 391, 428, 502(1), 504(11), 506(23), 507 569(64, 65, 66), 570(65), 571(69, (29), 508(42), 510(42, 45), 511(42, 47, 73), 572(74), 573(36), 575(73, 75, 84), 48), 512(51, 52), 513(59), 514(23), 515 578, 579, 580, 581 (65, 70), 516(70, 73), 517(69, 75), 518 Gossauer, A., 37(43, 45), 39(43), 103, 137 (22, 47, 48), 519(22, 48), 520(59), 522 (68), 744, 216(47), 219(59), 228(47), (59), 526(1, 107), 527(107), 529(1), 530 229(74, 76), 236(98), 247, 242, 245, (42), 531(11), 555(1, 11, 22, 42, 48, 59, 485(31), 499 70), 556, 537,538, 539

Hamilton, A., 161(68), 766 Higson, B. M., 279(175, 176), 282(177), Hamilton, A. L., 238(99), 245, 281(185), 292, 293, 336(25), 559 293 Hill, E. A., 379(114), 592 Hamilton, J. A., 432( 2, 3) , 433( 2, 3) , 439 Hill,H. A. O., 255(81, 82), 259, 311(69), (3), 441( 3), 442( 3), 449( 3, 39, 4 0), 451 312(69), 522, 336(27), 343(52, 59), 345 (39, 40), 453(39, 40), 460, 462 (59), 346(52), 347(52), 348(52), 349(52), Hamilton, R., 576(93), 582 350(52),351(52),353(59,66,67),354(52), Hamm, D. J., 426(105), 430 361(75), 362(52), 369(52), 389, 390, Hanaucr, R., 125(50), 143 391, 394(1), 395(1), 397(8), 404(22, 28), Hanna, M . L. , 527(38), 40 4(32), 405( 32), 407(1), 408(8), 409(1, 8, 60, 61), 412(60, 418(32), 425, 524(92), 538 67, 71), 413(61), 415(61), 418(68, 85), Hansen, H. J., 556(43), 580 420( 1,68),422(1,68),427,429,430, 439 Hanson, J., 538(61) (20a, 20b), 451(38), 452(38), 456(5, 6), Hanson, K. R., 562(52), 580 458(57),467,462,464(2,3, 4),467(5, 7), Hanzlik, J., 252(48), 288, 335(15), 388 468(7, 10), 469(2, 7,11), 471(3, 7), 472 Hardeggev, B , 212(33), 247 (7), 473(5, 7), 482(7, 27, 29), 483(3, 7), Harris, D. L., 153(31), 165 484(7, 29), 487(3, 27, 29, 40), 488(29), Harris, R. K., 477(20), 492(20), 499 490(2, 27, 29, 45, 50), 491(29), 492(7), Harrison, H. R., 75(67), 104 493(7), 494(7), 495(50), 496(5), 497(50), Harrison, M. J., 27 495, 499, 500, 527(110,112), 559, 558 Harrod, J. F., 404(24), 427 (48), 580 Harrowfield, B. V., 439(19), 440(24), 467 Hill, J. A., 343(53), 349(53), 390 % Hart, A. C, 156(53), 766 Hinze, R. P., 219(58, 59), 242 Hartshorn, A. J. , 92( 128), 106, 267(115), Hirai, K., 239(102), 245 290, 298(11), 320, 573(78), 557 Hitchcock, P. B., 77(69), 105 Hasemann, V., 468(13), 499 Hitchman, M. A., 439(18), 440(23), Hashimoto, N., 213(40), 247 467 Haslinger, E., 126(53), 744 Ho, K. S., 117(26), 120(26), 137(68), Hastings, A. B., 3(1), 4(1), 75 742, 744 Hausinger, R., 495(51), 497(51), 500 Ho, R. K. Y., 308(63), 522 Hawkinson, S. W., 35( 40), 103, 154(36), Hoard, J. L., 80(79), 105 765, 342(45),390 Hodder, O. J. R., 33(39), 75(67), 103,104, Hayon,E., 250(32), 257 208(24), 224(24), 247, 345(60), 390 Hayward, G. C, 314(78), 322,412(71),42P Hodgkin, D. C., 24(3, 4), 25(3), 26(11, Heeg, M. J., 85(86, 91, 94), 102(86), 105 12, 13, 14, 15, 16, 17, 18, 19, 20), 27 Heger, I., 117(30), 742 (21), 28(22), 30(32), 33(34, 35, 36, Heise, K. P. , 216( 47), 219( 59), 228(47), 37, 38), 40(16), 47(22), 54(54), 69(59), 247, 242 72(54), 75(67, 68), 78(76, 77, 78), 102, Helgeland, K., 228(72), 242 103,104,105, 110(7), 747, 147(4), 764, Hellmann, G., 548(10), 575 202(1, 3), 204(1, 10), 205(15, 16), Henderson, R. J., 373(90), 391 207(15, 20), 223(67), 224(67), 231 Henglein, A., 573(76), 557 (88), 234(17), 240, 242, 243, 246 Henry, R. A., 706(118) (1), 256, 296(1), 313(75), 579, 522, Hensens, O. D., 353( 67), 390, 456(5, 6) , 342(43, 44, 45, 47, 48, 49), 344(47), 467(5, 7) , 4 68(7), 469( 7), 471( 7), 472 347(47), 559, 390, 407(59), 422(100), (7), 473( 5, 7) , 482( 7), 483( 7), 484(7), 429, 430, 432(5), 460, 467(9), 472 492(7), 493(7), 494(7), 496(5), 495 (9), 482(9), 495 Herbst, M. M., 449(31), 467, 571(69), 557 Hodgson, G. L., 117(29), 118(29), Hesse, D , 404(26), 427 742 Hester, R. E., 344(55), 390, 398(10), 427 Hoffbrand, A. V., 161(70), 163(83), Hicks, P. R., 381(119), 382(119), 392, 452 766, 767 (44), 453(44), 454(44), 457(44), 462, Hoffman, M. Z., 250(32), 257 559(51), 580 Hoffman, P. J., 455(55), 462

Hogenkamp, H. P. C 30(31), 54(53), Hussein, H. A. A., 161(70), 766 705, 104, 147(3), 164, 247(10), 251 (28), 255(79), 267(114), 268(124, 126, Iannarella, L., 338(35), 389 127, 128, 129), 287, 289, 290, 291, Ihara,M., 112(14), 113(14), 114(14b), 297(3, 4), 300(20), 301(24), 303(20, 116(25), 117(25), 120(25b), 742, 27) , 304(24), 305(45, 47), 306(51, 55, 218(56), 242, 482(25), 499 56, 57), 307(55), 310(55, 64), 312(47, Ikeda, K., 116(23), 742, 338(33), 72), 313(55, 74, 76), 320, 321, 322, 389 331(11), 353(68), 354(69, 70), 388, Imfield, M., 115(17), 126(55), 132(59), 390, 391, 404(29), 405(46), 418(29, 742, 744, 318(93), 323 31), 427, 428, 432(1, 3), 433(3), 439 Ing, S. Y. S., 228(73), 242 (3), 440(22), 441(3), 442(3), 449(3, Ingold, K. U., 567(58), 580 33, 34), 455(55), 460, 461, 462, 478 Ingraham, L. L., 248(12), 249(17), 256 (21), 482(24, 28), 486(36), 487(24, (89), 257(89), 266(89), 284(17), 287, 28) , 488(21, 24), 489(21, 24), 490 289, 302(33), 314(77), 321, 322, 398 (21), 492(46), 493(24, 28), 495(21, (11), 427, 534(155), 547, 556(45), 51), 497(24, 51), 499, 500, 504( 14), 564(53), 575(86, 89), 580, 581, 508(37), 524(37, 91), 525(37), 527 582 (114, 118, 119), 529(127), 536, 538, Ingram, D. J. E., 461(14) 539, 540, 545(3), 549(15), 552(20), Inhoffen, H.-H., 125(50), 744, 216(47), 554(32), 578, 579 219(58,59), 228(47), 247 Holiday, E. R., 204(8), 215(8), 240 Irion, E., 161(66), 766, 303(34), 312(71), Holland, H. L., 282(192), 284(192), 293, 316(87), 527, 322, 323 534(151), 541, 549(14), 575(84), 578, Irvine, D. H., 412(66), 429 581 Irwin, A. J., 120(40), 123(40), 126(40), Holland, R. J., 252(42, 43), 253(42, 43), 127(52), 133(62), 134(62), 135(62), 254(43), 255(43), 256(43), 267(118), 137(62), 745, 744 288, 291, 300(15), 307(15), 316(84), Ishikawa, Y , 455(53), 456(53), 320, 323, 363(82), 365(85), 391, 506 462 (24) , 507( 28), 524( 24), 527( 116), 536, Itoh, N., 338(33), 389 539 Iwamoto, H., 150(19), 161(19), Hollenstein, R., 115(18), 116(25), 117 764 (25) , 120(25b),742 Holloway,M. R., 576(91), 582 Jackson, B., 163(83), 767 Holm, R. H., 438(16), 461 Jackson, W. R., 394(1), 395(1), 407(1), Holmes, A., 202 (5), 209( 5), 212( 5), 214 409(1), 420(1), 422(1), 427 (5), 217(5), 227(5), 230(5), 240 Jacobsen, D. W., 163(82), 767, 267(118), Holmes, S., 247(10), 287 297, 300(15, 16), 307(15), 320 Holt, E. M., 706(118) Jaffe, H. H., 340(38), 389 Horig, J., 110(3), 120(3), 747 Janata, E., 573(76), 557 Horn, U. , 282( 192), 284( 192), 293, 534 Jaselskis,B., 418(87), 430 (151), 547,575(84), 581 Jauernig, D., 239(101), 245 Horsley, W. J., 489(42), 500 Jencks, W. P., 337(29), 352(63), 389, Hoskins, B. F., 78(73), 105 390 Hosozawa, S., 118(34), 745 Jensen, F. R., 254(75), 260(98), 268 Howard, J., 539 (130, 131), 289, 290, 291, 317(88), Huennekens, F. M., 147(10), 157(57, 525, 512(57), 523(88), 525(57), 59), 158(57), 159(62, 63), 161(63), 538 162(75, 76, 77), 163(82), 764, 766, Jenson, L. H., 706(123), 117(26), 120 167, 267(118), 297, 300(15, 16), 307 (26), 742 (15), 320 Joblin, K. N., 298(9), 299(13), 320, 553 Huie, B. T., 280(180), 293 (26), 576(91), 579, 582 Hunt, E., 117(29), 118(29), 742 Johansen, J. T., 468(13), 499

Johnson, A. W., 110(5, 7), 120(5), 747, Kammerer, P., 117(30), 143 147(7), 156(45), 164,165, 202(2), 203 Kamper, J., 26(14, 15), 102, 110(7), 141, (37), 204(2, 11), 213(37), 215(2, 11), 204(10), 2 05(16), 240, 407(59), 429 216(43, 45), 218(2, 55), 220(2, 11, Kamper, M. J., 26(17, 19, 20), 27(21), 55), 225(11), 226(11), 227(11), 230 103, 342(43), 389 (79), 231(11), 234(79, 80), 236(11), Kang, J., 377(98), 379(105,107), 392, 532 238(11, 37, 99), 240, 241, 242, 243, (143,144,145), 540, 565(56), 566(56), 246(3), 252(3), 254(68, 69), 266(3), 580 267(112, 115), 271(147), 277(3), 281 Karrer, P., 204(9), 241 (49) (185, 186), 286, 289, 290, 292, 293, Kasha, M., 402(20), 403(20), 406(58), 297(6), 298(7, 9, 11), 302(29, 32), 407(58), 427, 428 305(46), 306(54), 318(54), 320, 321, Kaska,W. C, 276(161), 292 335(19), 340(37), 389, 417(81), 418 Katada, M., 485(34), 499 (89), 419(89), 429, 430, 508(34), 524 Kato,T., 154(38), 165 (34), 536, 538, 549(13), 553(26), 573 Katz, J. J., 112(12), 142 (78), 576(91), 578, 579, 581, 582 Katz, R. N., 282(191), 293, 297(5), 307 Johnson, E. A., 277(165), 292, 418(91), (5), 316(86), 320, 323, 575(88), 581 430 Kaufman, E. J., 253(58, 59), 288 Johnson, M. D., 226(93), 246(2), 256(2, Kemball, C , 252(49), 288 90), 257(93), 261(93), 263(93, 104), Keese, R., 212(35, 36), 220(35, 36), 241, 265(93), 266(108), 267(108), 268(134), 345(61), 390 269(136), 277(166), 285(204, 205), Keljo, D. J., 248(21), 287 286, 286(204, 205), 289, 290, 291, 294, Kemp, T. J., 284(198), 293, 303(39), 300(18), 320, 330(7), 335(7), 364(7), 316(39), 321, 532(136, 137, 138), 534 365(7), 381(118), 388, 392, 504(8), (149), 540, 541, 553(24), 571(69, 73), 516(74), 517(8), 525(100, 101), 526 572(74), 575(73, I S ) , 579, 581 (100), 527(101), 536, 538, 539, 551 Kempe, U. M.. 269(139), 291, 377(101), (18) , 568(63, 66), 569(63, 66, 67), 570 392, 533(146,147, 148), 540, 564 (63), 579, 580, 581 (54), 580 Johnson, R. A., 532(134), 534(134), 540 Kennedy, F. S., 297(120), 303(35), 311 Jones, C, 144(11) (69), 312(69), 321, 322, 405(45), 428, Jones, H. E., 122(44), 143 490(43), 500, 526(105), 527(110), 529 Jones, I. D., 426(105), 430 (105), 539 Jones, J. R., 468(12), 499 Kennedy, S. F., 303(36), 527 Jones, K., 122(46), 123(46), 125(46), 126 Kennedy, S. M., 267(115), 290, 298(11), (46), 128(46), 135(66), 143,144 320, 573(78), 581 Jones, W. H., 26(8), 102 Kerr, J. A., 509(44), 531 (133), 537, 540 Jonsen, J., 228(72), 242 Kerwar, S. S., 156(51), 166, 548(11), 550 Jordan, P. M., 118(34, 39), 143 ( 1 1 ) , 578 J0rgensen, C. K , 409(64, 65), 429 Khanna,P. L., 261(102), 290 Jorin, E., 441(25), 442(25, 26), 458(60), Kharasch, M. S., 540(141) 459(60), 461, 462 Kimball, M. E., 276(161), 292 Julita,P., 152(26), 154(26), 165 King, N. K., 458(56), 462 King, T. J., 77(70), 105 Kaczka, E., 239(104), 243 Kishimoto, S., 121(41), 745 Kajiwara, M., 112(13), 115(19), 133(19), Kiskis, R. C., 268(131), 297, 512(57), 137(68), 142,144, 218(52), 241, 473 525(57), 537 (19) , 479(19), 480(19), 481(19), 499 Kistenmacher, T. J., 59(85), 85(85), 86 Kallen, R. G., 248(14, 20, 21), 249(19), (85), 105 287, 289, 308(62), 311(67), 322, 527 Kitchin, J. P., 317(91), 525 (117), 529(117), 539 Klein, H., 137(68), 744 Kamenar, B., 78(72, 73), 105 Klem, A., 249(26), 287 Kamin, H., 122(45), 125(45), 128(45), 143 Klioze, S., 117(26), 120(26), 742

Kochi, J. K., 379(111, 115), 392, 556 Laland, P., 249(26), 287 (41), 580 Laland,S., 228(72), 242 Kohlmiller, N. A., 495(51), 497(51), Lamm, F. P., 527(116), 539 500 Lappert, M. F., 267(115), 290, 298(9, Kohnle, J., 80(80), 105, 419(95), 430, 11), 320, 553(26), 573(78), 576(91) 502(2), 535 579, 581,582 Koketsu, N., 246(4), 254(62), 255(62), Larkin, J. P., 573(75), 581 256(62), 257(62), 263(62), 265(62), Law, D. Y., 297(119) 286, 289 Law, P. Y., 298(10), 320, 469(15), 499 Kbnigk,E., 161(71), 166 Lawson, W. B., 228(70), 242 Koniusky, F. R., 25(5), 102, 239(104), Lee,E., 116(24), 117(26), 120(26), 742 243 Lee, h .,538 Kopf, J., 92(127), 106 Lee, L. P., 277(168), 292, 308(63), 322 Koppenhagen, V. B. , 37(41), 40(47, 48) , 362(77), 365(77), 369(11), 391, 398 ' 72(60, 6 1), 74(41), 103,104, 211(27, (14), 404(14), 406(14), 419(14), 427, 28,29, 30), 241, 485(32), 499 432(7), 439(7), 458(58), 460, 462, Kosower, E. M., 409(63), 429 508(36), 524(36), 536, 553(22), 579 Krasna, A. J., 149(16), 164 Lee, S. L., 117(26), 120(26), 142 Krautler, B., 212(33), 241 LeGates, R., 248(18, 19), 249(18), 271 Krebs, T., 377(101), 392, 533(146, 147, (18), 270(145), 276(145), 283(18), 148), 540, 564(54), 580 287, 292 Kriemler, H.-P., 123(47, 48), 125(47, 48), Legrand, M., 420(99), 430 126(47), 127(47), 128(47), 129(59), Leigh, G. J., 549(10,578 130(47), 132(48, 57), 133(62), 134 Lenhert, P. G., 30(27, 28, 30), 41(30), (48, 57, 62), 135(57, 60), 137(57, 62), 54(28), 59(28), 61(28), 64(28), 80 143,144 (81), 85(88), 87(88), 88(88), 103,105, Krodel, E. K., 65(56), 104, 282 110(7), 747, 147(4), 764, 207(18), 208 (188), 283(188), 284(188), 293, (18), 240, 246(1), 286, 341(42), 342 579(11) (42), 344(42), 354(42), 355(42), 359 Krouwer, J. S , 576(92), 578(U, Id), (42), 389, 391(14), 398(12), 427, 432 582 (6), 442(6), 460, 467(8), 472(8), 490 Krueger, G. J., 706(105) (8), 498, 505(21), 506(21), 514(21), Krusic, P. J., 379(115), 392 536, 550(16), 551(16), 579 Kuehl, F. A., 218(53, 54), 241, 242 Lenoir, D., 255(76), 261(76), 289 Kuhlmann, K. F., 477(20), 492(20), 499 Lenp, J., 404(44), 428 Kuhn, H., 396(2), 398(2), 400(18), 401 Leont'eva, Ye. V., 379(113), 392 (2, 18), 402(21), 403(21), 420(21), Leopold, J. G., 318(95), 323 427 Lerner, D., 404(42), 418(42), 419(42), 428 Kurganov, B. I ., 305(49, 50) , 306(49, Levitin, I. Y., 516(72, 73), 538 50), 321 Lewis, J., 539 Kustanovich, I. M., 284(202), 285(202), Lewis, N. G., 133(61), 134(61), 135(61), 293, 575(85), 581 137(61), 744 Kwiatek, J., 292(163), 538 Lexa, D., 252(46), 253(46), 288, 318(92), Kyaw, M., 218(97), 319(97), 323, 376 323, 337(26), 364(84), 389, 391, 506 (92), 391 (25), 514(25), 522(25), 536 Li, T. K., 423(102), 430 Laas, H., 2 16(47), 219(59), 228(47), Licare,T., 537 241, 242 Liebman, M., 47(50, 51, 52), 104 Ladd, J. N., 30(31), 54(53), 103,104, Lien, E. L., 297(119), 469(15), 499 296(2), 297(3), 312(73), 319, 320, Lindsey, J., 26(11, 15, 18), 102, 103,106, 321, 353(68), 390 205(16), 240, 342(44), 389, 407(59), Ladd,T. M., 156(47), 765 422(100), 429, 430, 467(9), 472(9), Lake, R. E., 85(90), 105 482(9), 498

Lindstrand, K., 147(6), 161(67), 164, MacKay, M., 110(7), 141, 407(59), 429 166 McKenna, W.,547 Linhard, M., 428(49) McKenzic, E. D., 279(175, 176, 177), Linnell, J. C, 161(68, 69, 70), 163(83), 282(177), 285(204), 286(204, 206), 166, 167 292, 293, 294, 336(25), 381 Lipscomb, J. D., 539 McKervey, M. A., 576(93), 582 Livant, P., 549(12), 578 McLaughlin, G. M., 77(69), 105 Ljungdahl, L., 161(66), 166, 303(34), McPhail, A. T., 106(116), 249(25), 254 321 (24), 278(25), 287 Lloyd, D., 212(34), 241 MacQuitty, J. J., 267(115), 298(11), 290, Lockman, B. L., 285(205), 286(205), 320, 573(78), 581 294, 525(100, 101), 526(100), 527 Madan, V., 260(98), 268(130), 290, 291, (101), 539 317(88), 323, 523(88), 538 Locwenstein, A., 490(45), 500 Magnuson, R. H., 516(73), 538 Lohaus,G., 213(38), 241 Mahcr, J. P., 273(152, 153), 292, 502(1), Long, K. M., 250(33), 287, 404(35), 406 511(47), 518(47), 526(1), 529(1), 535 (54), 418(35), 428 (1,47), 535, 537 Longworth, J. W., 426(107), 430 Mahoncy, M. J., 156(53), 166 Looney, F. D., 432(2, 3), 433(2, 3), 439 Maillard, P., 404(39), 405(39), 418(39), (3, 21), 441(3), 442(3, 21), 443(21), 419(39), 428, 553(23),579 444(21), 445(21), 449(3, 21), 458(56), Majerus, P. W., 268(121), 291 460, 461, 462 Maki, A. H., 438(16), 461 Loots, M., 512(52), 537 Mamalis, P., 352(64), 365(64), 390 Lovenberg, W., 163(84), 167, 254(71), Mann, B. E., 343(52), 345(59), 346(52), 289 347(52), 348(52), 349(52), 350(52), Lovtsova, A. N., 379(113), 392 351(52, 59), 353(59, 66), 354(52), Lowc,D. J.,299(13), J20 362(52), 369(52), 390, 397(8), 408 Lu, L.-Y., 278(173), 292 (8), 409(8), 418(85), 427, 429, 464 Lu, S. H., 110(3), 120(3), 141 (3), 469(3), 471(3), 482(29), 484(3, Luthy,J., 115(22), 142 29), 487(3, 29), 488(29), 490(2, 29), Lyles, D., 248( 14), 249( 14), 28 7, 308 491(29), 494(3), 498, 499 (62), 322 March, J., 337(28), 389 Lynen,F., 532(139, 140), 540 Margum, J. H., 163(78), 166 Marshall, D. R., 212(34), 247 Maag, H., 202(5), 209(5), 212(5), 213 Marsich,N., 317(90), 323 (40), 214(5), 217(5), 227(5), 230(5), Martella, J. P., 276(161), 292 240, 241 Martin, A. H , 272(150), 277(150), 292 McAuliffe, C. A., 388(3) Martin, H., 396(2), 398(2), 401(2), 427 McAuslan, B., 156(51), 166 Martin, J. C, 549(12), 578 Marwaha, L. K., 377(99), 379(99), Maccoll, A., 338(30), 389 392, 567(62), 580 McDonald, E., 111(8), 112(11, 14), 113 Marx, J. N., 258(96), 290 (14), 114(146), 115(18), 116(8, 25), Marzilli, L. G., 85(83, 85, 87), 117(25, 28, 29, 31, 32, 33, 35, 36, 37), 86(83, 85, 95), 88(83), 105, 118(28, 29, 33), 120(25b), 121(41), 273(156), 275(156), 292, 359 122(43, 46), 123(40, 43, 46), 125(43, (72), 375(72), 382(72), J97, 46, 51), 126(46, 51, 53), 127(28a), 491(47), 500, 505(18, 20), 506 128(46), 129(43, 56), 130(56), 132 (20), 518(80), 519(81), 531(18, (49, 60), 133(60, 61), 134(61), 135 20), 535(80, S I ) , 536, 538 (43, 60, 61), 137(61), 142, 143, 218 Marzilli, P. A., 273(156), 275(156), 292, (56), 242, 482(25), 499 518(80), 519(81), 535(80, 81), 538 McFadden, D. L., 106(116) Mason, H. S., 432(1), 460 Mackay, M ., 26( 14, 15) , 102, 204(10), Masuda, I., 406(55), 419(55), 428 205(16), 240

Matcham, G. W. J., 117(28, 32, 33), 118 Mildvan, A. S., 65(56), 68(57), 104, 382 (28,35,36,37), 127(28a), 132(60), (121), 392, 451(37), 462, 558(47) 133(60, 61), 134(61), 135(60, 61), 137 559(47), 579(11), 580 (61) , 142, 143,144 Miller, I. M., 116(23), 142 Math, V. B., 33(39), 103, 208(24), 222 Miller, I. W., 111(9), 142 (65), 223(65), 224(24), 234(65), 236 Milton, P. A., 494(49), 496(49), 500 (65), 241, 242, 345(60), 390, 485(33), Mingardi, M., 406(56), 428 499 Minghetti, A., 152(26), 154(26), 165 Mathews, D. M., 161(68, 69, 70), 166 Mitchell, T. R. B., 576(93), 582 Matsuda, A., 300(17), 320 Mok, C. Y., 503(5), 508(5), 524(5), 525 Matsumoto, H., 118(34), 143 ( 5 ) , 535, 554(28), 579 Matsumoto, J., 150(19), 161(19), Molander, G. A., 260(100), 290, 539 164 Mombelli, L., 144(10) Matt, J. W., 567(59), 580 Monkjaro, Y., 300(15), 307(15), 320 Mattern,C. F. T., 30(29), 103 Montejano, Y., 267(118), 291 Matwiyoff, N. A., 268(127, 128, 129), Montforts, S., 135(66), 144 291, 301(24), 304(24), 313(76), 320, Montgomery, L. K., 567(59), 580 322, 354(70), 391, 404(31), 418(31), Moore, F. H., 33(35, 36), 103, 205(15), 428, 478(21), 479(22), 482(24), 484 207(15), 240, 342(47), 344(47), 347 (22), 487(22, 24), 488(21, 24), 489 (47), 390 (21, 24), 490(21), 492(46), 493(24, Moore, F. M., 231(88), 243, 313(75), 48), 495(21,51), 497(24, 51), 499, 322 500, 552(20),579 Moore, K. W., 554(30), 555(30), 579 Mauck,L., 555(34), 579 Moore, M., 218(54), 242 Mayer, E., 344(55), 390, 398(10), 427 Morallee, K. G., 490(45), 500 Mays, M. J., 276(162), 292 Morley, G. G. D., 313(74), 322, 574(80), Meegan, M. J., 117(32, 33), 118(33), 581 143 Morris, H., 122(43, 46), 123(43, 46), 125 Meeks, B. S., 256(93), 257(93), 261(93), (43,46), 126(46), 128(46), 129(43), 263(93, 104), 265(93), 290 135(43), 143 Merienne, C, 256(74), 264(74), 289, Morris, H. R., 132(60), 133(60), 135(60), 304(42), 321, 364(83), 391, 404(37), 144 405(37), 418(37), 428, 511(49), 512 Moskophidis, M., 267(116), 290, 301(27), (55), 525(55), 537 320 Merle, G., 525(95), 539 Moss,T. H., 381(120), 392, 449(28, 32), Mervyn, L. , 147( 7), 156( 45), 164, 165, 450(32), 451(28, 32), 453(32), 461, 558 224(68), 242, 254(68, 69) , 2 67(112), (49), 580 271(147), 289, 290, 292, 429 Mueller, O., 268(123), 291 Messerschmidt, R. , 413( 72, 73, 7 4, 75, Muggleton, P. W., 271(147), 292 76), 415(72), 429 Miiller, G., 117(27, 30), 123(47, 48), 125 Mestroni, C., 254(63, 65), 256(91), 270 (47,48), 126(47), 127(47), 128(47), (91), 271(146), 277(170, 171), 280 129(57), 130(47), 132(48, 57, 59), 133 (91), 289, 290, 292, 301(28), 320, 336 (62), 134(48, 57, 62), 135(57, 62), 137 (24), 389, 502(3), 514(3), 525(99), (57, 62), 143,144(10), 150(18), 164, 526(109), 535, 537,539 235(90), 236(90), 243 Meyer, E. F., 241(25), Mullcr, N.,500 Meyer, E. F., Jr., 75(62, 63), 78(62), 80 Miiller, O., 148(14), 150(18), 164, 235 (62) , 104 (90), 236(90), 243, 254(67), 289, 429 Meyerstein, D., 574(81), 581 MUller, R. M., 212(33), 241 Michaely, W. J., 316(84, 85), 323 MUller, U. G., 429 Michna, H , 110(2), 120(2), 141, 231 Munch, E.,539 W) , 243 Munch-Peterson, A., 156(47), 165 Migliacci, A., 152(26), 154(26), 165 Murakami, M., 150(19), 161(19), 164

Murie,R., 239(103), 243 Obata, N., 202(5), 209(5), 212(5), 214 Murphy, M. J., 122(45), 125(45), 128 (5), 217(5), 227(5), 230(5), 240 (45), 143 Ochiai, E ., 250( 33), 287, 404(35), Murphy, S., 157(57), 158(57), 166 406(54), 418( 35), 428, 450(42), Myers, C, 156(52), 160(52), 166 462 Myerstein, D., 292(151) Ochiai, E.-L, 556(37), 578(94), 579, 582 Nardelli,M., 106(110) O'Connor, B. H., 33(36), 103, 205(15), Nardin, G., 343(51), 349(51), 360(51), 207(15), 240, 342(47), 344(47), 347 390, 505(16), 531(16), 536 (47), 390 Nath, A., 485(34), 499 Oester,M. Y., 125(50), 144 Naumberg, M., 253(53), 256(53), 257 Offenhartz, B. H., 396(3), 397(9), (53), 263(53), 265(53), 288, 524(90), 401(3), 427 538 Offenhartz, P. O., 397(9), 427 Needham, T. E., 268(127, 128, 129), 291, Ofner, S., 135(66), 144 478(21), 488(21), 489(21), 490(21), Ogawa,H., 317(89), 323 493(48), 495(21), 499, 500 Ogoshi, H., 246(4), 254(62), 255(62), Neier, R., 129(56), 130(56), 144, 239 256(62), 257(62), 263(62), 265(62), (102), 243 286, 289 Neler, R., 132(60), 133(60, 61), 134 Ohashi, Y., 88(96, 101, 102, 103), 89 (61), 135(60, 61), 137(61), 144 (104,115), 90(101), 105,106 Nelson, J. H., 106(11%) Ohgo, Y., 88(102, 103), 89(115), 106 Nemeth,S., 253(60, 61), 288 Ohta,H., 160(65), 166 Neri,C., 280(182), 293 Oikawa, T. G., 305(47), 312(47), 321 Nerone, A., 85(92), 105 Okada,K., 113(13), 142, 218(52), 241, Neta, P , 571(68, 71,72), 581 473(19), 479(19), 480(19), 481(19), 499 Netzel, T. L., 299(14), 320, 363(79), Oldfield, D., 297(6), 320 376(79), 391, 404(40), 405(40), 418 Oleson, H., 414(78), 417(78), 423(78), (40), 428 429 Neumann, E., 137(68), 144 Olivella, S., 567(60), 580 Newman, M. S., 231(86), 243 Olson, C. D., 440(23), 461 Nex0, E., 268(122), 291, 414(78), 417 Oltersdorf, U., 225(69), 228(69), 242 (78), 423(78), 429 Orgel, L. E., 338(30, 31), 389 Ng, F. T. T., 508(42), 510(42, 45), 511 Orme-Johnson, W. H., 381(120), 392, (42), 530(42), 535(42), 537 441(32), 450(32, 35), 451(32), 453 Nicholson, B. K , 298(9), 320, 553(26), (32), 455(35, 52, 53), 456(52, 53), 579 461,462, 558(49, 50), 580 Nocchi, E., 303(39), 316(39), 321, 508 Ostroy,F., 156(54), 166 (39), 525(39), 534(149), 537,541, 553 Overath, P., 532(139, 140), 540 (24), 571(69, 73), 575(73), 579, 581 Overend, W. R., 203(37), 221(37), 213 Nockolds, C. E., 33(36), 103, 33(34, 36), (37), 238(37, 99), 241, 243 103, 205(15), 207(15), 240, 342(47), 344(47), 347(47), 390 Page, J. E., 25(7), 102 Nome, F., 304(43), 321, 409(62), Pailes, W. H., 251(28), 287, 303(37), 321, 429 597(71), 405(46), 428, 524(91),538 Nordlov,H., 118(34), 143 Palmieri,C. G., 706(110) Nordmeyer, J. P., 249(27), 287, 301(26), Pannhorst, W., 87(97, 99), 88(97, 99), 320, 413(72, 73, 74, 75, 76), 415(72), 105, 269(139), 270(141,142), 297, 429 379(104, 106), 392, 533(146, 147, Norman, R. O. C, 532(135), 534(135), 148), 540, 565(57), 580 540, 573(75), 581 Parfenov, E. A., 282(189, 190), 284(199, Nussbaumer, C., 144(10) 200, 201, 202, 203), 285(200, 202), Nyholm, R. S., 330(38), 389 293, 294, 549(14), 575(85), 578, 581

Park Y., 275(159), 292, 335(21), 389 Pilbrow, J. R., 381(119), 382(119), 392 Parker, I. H., 438(17), 439(17), 467 432(8), 433(9), 434(9), 437(9,10), ' Parker, L. F. J., 12(2), 13(2), 15, 25(7), 438(12a, 12b), 439(8, 9, 19, 21), 440 102, 110(5), 120(5), 141, 204(11), (9, 24), 442(21), 443(21), 444(21), 215(11), 220(11), 225(11), 226(11), 445(21), 449(21), 452(50, 51), 453 227(11), 230(79), 231(11), 234(79), (9, 44, 50, 51), 454(44), 457(9, 44), 236(11), 238(11), 240, 418(80), 429 460, 461, 462(59), 559(51), 580 Parry, R., 469(14), 499 Pilling, D., 26(19), 103, 342(43), Patchornik, A., 228(70), 242 389 Pawelkiewicz, J., 154(38), 165, 230(81), Pinnock, H. A. , 245( 100), 246 242, 267(113), 290 (3), 252(3), 266(3), 277(3), Payne, M. D., 85(91), 105 286, 302(32), 527 Pearson, R. G., 250(36), 288 Poe, M., 343(58), 344(58), 349 Pellizen, A., 502(3), 514(3), 555 (58), 350(58), 354(58), 390, Pellizer, G., 254(65), 256(91), 270(91), 469(16), 471(17), 486(17), 280(91), 289, 290, 301(28), 320, 336 487(17), 499 (24), 389, 490(45), 500 Porter, G. B., 406(56), 428 Pencovici, M., 248(14), 249(14), 287, Porter, M. W., 24(3), 25(3), 102 308(62), 322 Pospelova, T. A., 267(111), 290, 305 Penley, M. W., 307(59), 322, 490(50), (49, 50), 306(49, 50), 527 495(50), 497(50), 500 Postgate, J. R., 122(44), 745 Peng, S., 335(21), 389 Poston, J. M., 147(8), 155(8), 764, 528 Peng, S.M., 275(159), 292 (121), 559 Perego,G., 280(182), 293 Poznanskaya, A. A., 267(111), 290 Perlman,D., 306(52), 321 Pratt, J. M., 158(60), 766, 228(71), 242, Perree-Fauret, M., 251(39), 279(179), 288, 255(77, 81, 82, 83), 289, 300(19, 21), 293 303(21), 311(69), 312(69), 314(78), Perrin, D. D., 277(172), 292 320, 322, 329(1, 2, 4), 330(2, 6), 333 Perrin,D. R., 277(172), 292 (1,2, 12), 335(2, 4, 6, 14,16), 336 Perrotti, E., 280(182), 293 (2, 27), 337(2), 342(2), 343(2, 52, 53, Pesaro, M., 236(96), 247(39), 243 54), 344(2, 54), 345(2, 59), 346(52), Peterkofsky, A., 156(44, 49, 50), 159 347(2, 52), 348(52), 349(2, 6, 52, 53), (49), 160(64), 163(50), 165,166 350(2, 52), 351(2, 52, 54, 59), 352(54), Petersen, R. L., 485(34), 499 353(2, 54, 66), 354(2, 52), 355(2, 54), Petrocine, D., 115(19), 133(19), 742 357(54), 358(54), 359(2, 54), 360(54), Petrova, R. G., 556(42), 580 361(4, 6, 75), 362(52, 54, 78), 363(2), Petrow, V., 26(9), 102, 204(8), 215(8), 364(2, 54), 365(54, 86), 366(2, 54), 367 240, 352(64), 365(64), 390 (6), 368(54), 369(52), 371(54), 373(90), Pezacka, E., 154(39), 765 374(2), 376(54), 377(4), 379(78), 380 Pfaltz, A., 212(33), 221(61), 239(102), (86), 381(4), 385(4), 386(4), 388, 389, 247, 242, 243 390, 391, 394(1), 395(1), 404(22, 27, Pfenninger, A., 744(71) 28, 33, 34), 405(34), 407(1), 409(1, 60), Pfiffner, J. J., 72(60, 61), 104, 211(27, 412(27, 60, 67, 69, 71), 413(61), 415 28, 29, 30), 228(73), 247, 242 (61), 418(33, 34, 68, 85), 419(69, 97), Phelan, P. F., 273(154, 157), 275(157), 420(1, 68), 422(1, 68), 427, 428, 429, 292, 518(22), 519(22), 535(22), 536 430, 439(20a, 20b), 464(2, 3, 4), 468 Phillips, C. S. G., 338(32), 339(32), 389 (10, 11), 469(2, 11), 471(3), 482(26, 29), Phillips, G. O., 318(94, 96, 97), 319(97), 484(3, 26, 29), 485(26), 487(3, 26, 39), 323, 376(91, 92), 391 488(29), 490(2, 26, 29, 50), 491(29), Pickworth, J., 26(11), 702, 26(11, 12,15, 492(26), 494(3), 495(50), 497(50), 498, 16), 40(16), 102,103, 110(7), 747, 499, 500, 504(6, 9), 508(9, 35), 524(35), 202(1), 204(1, 10), 205(16), 234(17), 527(110), 535, 556, 539, 567(61), 580 240, 342(48, 49), 390, 407(59), 429 Pribanic,M., 335(16), 389

Prince, R. H., 266(106), 290, 539 Renz, P., 110(3), 120(3), 141, 152(22, Pritchard, D. E., 500(44) 23), 153(22, 35), 154(35), 165, 216 Pritchett, J., 532(135), 534(135), 540 (44), 226(44), 241 Prosen, R. J., 26(12, 15, 16), 40(16), 103, Retey, J., 87(98, 99, 125), 88(98, 99), 202(1), 204(1), 205(16), 234(17), 240 105,106, 115(22), 142, 261(101), 269 Prout,C. K., 78(72, 73), 105 (137,139), 270(141, 142), 290, 291, Pryde, L. M., 118(34), 143 377(96, 101, 102), 378(102), 379(104, Pullman, B., 396(4), 398(4), 427 106), 381(102), 384(102), 385(102), Puxeddu, A., 250(35), 256(91), 270(91, 391, 392, 533(146, 147, 148),540, 143), 271(143), 280(91), 290, 336(24), 545(4), 558(4, 46), 564(54), 565(57), 389, 514(61, 62), 537 577(4), 578, 580 Puxeddu, E., 502(3), 514(3), 535 Reutov,0. A., 379(112), 392 Reynhardt, E. C., 706(105) Quadros, E. V., 161(68, 69), 163(83), Rhee,S. G., 352(65), 390 166,167 Ribiero, A., 308(63), 322 Que, L , 559(104) Ricchiero, F., 404(42), 418(42), 419(42), Quillivia, R., 300(18), 320 428 Richards, J. C., 404(43), 428 Radmer, R., 118(38), 143 Richards, J. H., 449(31), 467, 554(30), Radom,L., 452( 47), 462, 532(136, 137, 555(30), 571(69), 579, 581 138), 540, 556(36), 557( 36), 558( 36), Richardson, K., 243(100) 559(36), 573(36), 579 Rickes,E. L., 25(5), 102, 239(104), 243 Rahn,R. O., 426(107), 430 Ridley, W. P., 539 Raleigh, J. A., 231(87), 233(87), 243 Ridsdale, S., 255(82), 289, 490(50), 495 Ramaseshan, S., 33(34), 103 (50), 497(50), 500 Randaccio, L., 85(82), 86(82, 95, 111), Ridsdale, S. C., 311(69), 312(69), 322, 87(112), 88(82), 105, 106(106, 107, 527(110), 539 108, 109), 343(51), 349(51), 359 Rietz, P., 231(84), 243 (72), 360(72), 375(72), 382(72), Ritari, S. J., 163(80), 767 390, 391, 505(16, 17, 18, 19, 20), Robertson, J. H., 26(11, 12, 15, 16), 28 506(20), 531(16, 17, 18, 19, 20), 531 (24), 102, 103, 202(1), 204(1), 205 (20), 536 (16), 234(17), 240, 407(59), 429 Randacew, L., 491(47), 500 Robinson, J. A., 122(46), 123(46), 125 Rapp, P., 110(2), 120(2), 141 (46), 126(46, 53), 128(46), 143,144, Rapp, R., 110(2), 120(2), 141, 225(69), 270(140), 297 228(69), 231(89), 239(101), 242, 243 Roche, J. S., 271(149), 272(149), 292 Rasetti, V., 135(66), 144 Roche, T. S., 246(6), 271(6), 287, 335 Redfern, J. R., 218(56), 242, 482(25), (13), 389, 515(70), 516(70), 535(70), 499 538 Redfield, B. G., 156(44, 50), 163(50), Rodrigo, R. , 21 6(45), 247, 29 7(6), 302 165,166 (29), 306( 54), 318( 54), 320, 321 , 418 Redmond, J. W., 115(21), 142, 204(12), (89), 419( 89), 429, 430, 508(34), 524 212(12), 221(62), 231(87), 233(87), (34), 536 235(62), 236(93), 240, 243 Roewer,G., 553(27), 579 Reenstra, W. W., 352(63), 390 Ronzio, R. A., 152(27), 765 Reetz, M. T., 556(40), 580 Rooney, J. J., 576(93), 582 Rehorek,D., 553(27), 579 Rosales, F., 163(80), 767 Reisenhofer, E., 250(35), 256(91), 270 Rose, I. A., 562(52), 580 (91,143), 271(143), 280(91), 288, 290, Rosen, C. G., 526(105), 529(105), 539 291, 336(24), 389, 502(3), 514(3, 61, Rosenberg, L . E., 156( 53, 55) , 157( 56), 62), 535, 537 766 Rempel, G. L., 508(42), 510(42, 45), Rosenblum,C., 1 11(9), 742, 14 9(16), 511(42), 530(42), 535(42), 537 764

Rosenthal, D., 122(45), 125(45), 128 Schevlin,P. B., 556( 43), 580 (45), 143 Schiebel, H. M., 219(59), 242 Rowe, J. N., 564(53), 580 Schilling, W., 202(5), 209(5), 212(5), Rubin, E. M., 363(82), 391 214(5), 217(5), 227(5), 230(5), Rubison, K. A., 241(31), 426(104), 430 240 RUchardt,C, 548(10), 578 Schindler, O., 419(93), 430 Rudakova, I. P., 255(78), 267(109, 110, Schlecht, M., 268(123), 291 117), 285(117), 289, 290, 298(8, 12), Schlingman, G., 485(32), 499 299(12), 305(49, 50), 306(49, 50), 320, Schlingmann, G., 40(48), 104 321, 363(80, 81), 391, 513(58), 537, Schmid, H., 204(9), 240, 241(49) 573(77), 581 Schneider, P., 202(5), 209(5), 212(5), Ruoff,G., 239(101), 243 214(5), 217(5), 227(5), 230(5), 240 Rush, J. E.,289(S6),289, 306(55), 307 Schneider, P. W., 273(154), 292 (55), 310(55), 313(55), 322, 527(114), Schneider, Z., 154(40), 155(40), 165 539, 549(15),579 Schonland, D. S., 461(14), 461 Russell, G., 554(31), 579 Schrauzer, G. N., 80(80), 105, 109(1), Russell, G. A., 404(23), 427 141, 158(61), 166, 240(21), 246(7), Ryel, E. M., 156(54), 166 247(8, 9), 248(13), 250(30, 31), 251 (13), 252(9, 42, 43), 253(30, 42, 43, Sadler, P. J., 487(40), 500 56), 254(31, 43, 70), 255(43), 256 Saito,T., 276(164), 292 (8, 43, 88), 257(94, 95), 258(31, 97), Sakami, W., 163(80), 167 262(103), 263(103), 269(8), 277(13, Sakrikar, S., 282(192, 193), 284(192), 168, 169), 278(13), 282(191), 283(88), 293, 534(151, 153),541, 575(84), 287, 288, 289, 290, 292, 293, 297(5), 581 300(22), 301(22), 302(22, 31), 303 Salama,S., 343(57), 390 (22), 304(40, 41), 305(48), 307(5, 48, Salem, L., 398(15), 400(15), 411(15), 58), 308(63), 311(48, 58, 66, 68), 312 419(15), 427, 530(131), 540, 556(38), (48), 313(31, 58), 314(31), 316(84, 85, 562(38), 564(38), 576(38), 579 86), 320, 321, 322, 323, 351(62), 352 Sander, E. G., 337(29), 389 (62), 357(62), 358(62), 362(62, 77), Sando, G. N., 306(56), 322, 331(11), 363(82), 364(62), 365(77, 85), 366(87, 388, 455(55), 462, 529(127), 540, 545 88), 367(62), 368(62), 369(62, 77), 370 (3), 578 (62), 371(62), 373(88), 376(88), 390, Sands, R. H., 382(122), 392, 450(41), 391, 397(5), 398(13, 14), 404(13, 14, 451(141), 453(41), 454(41), 462, 558 30), 406(14), 418(30), 419(14, 30, 95, (47), 559(47), 580 96), 427, 430, 432(7), 439(7), 458(58), Sasada, Y., 88(101, 102, 103), 89(104, 460, 462, 502(2), 506(24), 507(28, 33), 115), 90(101), 105, 106 508(36), 511(50), 518(78), 523(87), Sato, K., 461(29), 545(5), 578 524(24, 33, 36), 525(33), 527(115, 116), Satoh, F., 116(25), 117(25), 120(25b), 529(115), 530(129, 130), 535, 536, 537, 121(41), 142, 143 538, 539, 540, 547(7), 549(7), 551 Saunders, J., 117(29), 118(29), 142 (19), 552(21), 553(21, 22), 559(7), Saveant, J.-M., 252(46), 253(46), 318 571(70), 575(88), 577(7), 578, 579, (92),323, 337(26), 364(84), 389, 391, 581 506(25), 514(25), 522(25), 536 Schreiber, J., 202(5), 209(5), 212(5), Schaefer, W. P., 280(180), 293 213(40), 214(5), 217(5), 227(5), 230 Schaeffer, E.,280(183, 184), 281(183, (5), 240, 241 184), 293 Schreiner, A. F., 426(105), 430 Schaffler, J., 261(101), 290 Schulten, H. R., 219(59), 242 Schaffner, T. J., 240(19) Schwartz, S., 116(23), 142 Scheffold, R., 236(96), 243 Schweiger, A., 441(25), 442(25, 26), Schepler, K. L., 382(122), 392, 450(41), 458(60), 459(60), 461, 462 451(41), 453(41), 454(41), 462 Scopes, P. M., 222(66), 242

Scott, A. I., 112(13), 113(16), 115(19), Shimizu, S. , 253( 57), 288, 301(25), 302 116(24), 117(26), 118(34), 120(26,40), (30), 311( 65), 320, 321, 322, 508(38), 123(40), 126(40), 127(52), 133(19, 62), 522(84), 524(38), 525(38), 536, 538 134(62), 135(62), 137(62, 68), 742,143, Shmyrev, I. K., 284(199), 295,549(14), 144, 218(52), 241, 379(105, 107), 392, 578 393, 473(19), 479(19), 480(19), 481(19), Shoemaker, C. B., 26( 15), 103,205(16), 486(37), 499, 500, 552(144, 145), 540, 240 565(56), 566(56), 580 Shoolery, J. M., 127(52), 144 Seek, J. A., 363(82), 391 Shoolery, J. N., 120(40), 123(40), 126 Seehra,J.S., 118(39), 143 (40), 745 Segal, G., 398(15), 400(15), 411(15), 419 Shulman, R. G., 426(107), 430 (15), 427, 530(131), 540, 556(38), 562 Shunk,C.H., 218(53), 247 (38) , 564(38), 576(38), 579 Shveima, J. S., 525(97, 98), 559 Segnitz, A., 295(178) Sibert, J. W., 247(9), 251(9), 252(9), 254 Seible, J., 377(96), 391, 545(4), 558(4), (70), 287, 288(31), 289, 300(22), 301 577(4), 578 (22), 302(22), 303(22), 305(48), 307 Seki,H., 318(93), 525 (48), 311(48, 68), 312(48), 320, 321, Sell, C. S., 284(198), 295, 452(48), 462, 322, 362(77), 365(77), 366(87), 369 532(136, 137, 138), 534(136), 540, (77), 597, 398(14), 404(14, 30), 406 572(74), 575(75), 581 (14), 418(30), 419(14, 30), 427, 507 Sellars, P. J., 268(125), 284(198), 291, (33), 508(36), 524(33, 36), 525(33), 293, 381(116), 592, 452(48), 462, 553 530(129), 536, 540, 553(22), 579 (24), 568(64, 65, 66), 569(64, 65, 66), Siebert, H., 425(47) 570(65), 571(69), 572(74), 575(75), Siegel, L. M., 120( 40), 122( 45), 123( 40), 579, 580, 581 125 (45), 126(40), 127 ( 5 2), 128(45) ,745, Sellers, P. J., 303(39), 316(39), 321, 508 744 (39) , 525(39, 97, 98), 532(136, 137, Sigan, A. L.,55#(68a, b) 138), 534(136), 557, 559, 540 Silverman, R. B., 248(15, 16), 281(15, 16, Septe, B., 404(36), 405(36), 406(36), 187), 282(15, 16,187,188,194), 283 418(36), 419(36), 428 (187, 188,195,196, 197), 284(188, Seyler, J. K., 292(163) 197), 287, 293, 315(79, 80, 81, 82, 83), Shapiro, M., 377(98, 99, 103), 379(99), 316(82, 83), 522, 525, 534(152, 154, 592, 532(142, 143), 540, 564(55), 565 156), 547, 575(83, 87), 557 (55), 566(55), 567(62), 580 Simandi, L. I ., 248( 23), 252( 23, 47, 50, Shatkina,T. N., 379(112, 113), 592 51), 253(47, 60, 61), 287, 288 Shaw, N., 147(7), 156(45), 164, 165, Sinke,G. C., 509(43), 557 216(43), 241, 254(68, 69), 267(112), Sinn, E., 92(128), 106 271(147), 289, 297(6), 290, 292, Skinner, H. A., 508(40), 557 298(7), 305(46), 320, 321, 429 Skyring,G.W., 122(44), 745 Sheldrick,G.M., 70(5(117), 266(106,107), Smith, C., 270(145), 276(145), 292 290 Smith, E. L., 25(6, 7), 102, 110(5), 120 Sheldrick, W. S., 37(41, 42, 43, 44), 39(43), (5), 747, 147(5, 7), 153(29), 156(45), 40(42, 47), 74(41, 42), 103,104, 229 163(81), 764, 765, 767, 202(2), 204 (74), 230(78), 242 (2, 11), 215(2,11), 218(2), 220(2,11), Shelton, G , 77(70), 105, 281(185), 295, 225(11), 226(11), 227(11), 230(79), 340(37), 389 231(11), 234(79), 236(11), 238(11), Shemin,D., 111(9, 10), 112(12), 218(51), 240, 254(68, 69), 267(112), 271(147), 142, 241 289, 290, 292, 418(80), 429 Shepler, K. W., 558(47), 559(47), Smith, L. E., 12(2, 3), 13(2), 75 580 Smith, S. G., 490( 50), 49 5(50), 497( 50), Shermin, D., 486(39), 500 500 Shida, T., 318(93), 525 Smith, T. A., 156( 52), 160( 52), 7 66, 548 Shima, K., 406(55), 419(55), 428 (11), 550(11), 578

Smith, T. D. , 3 81(119), 382( 119), 592, Stotter.N. E., 106(111) 438(12a, 12 b), 452( 44), 45 3(44, 50, Stout, G.H., 106(123) 51), 454(44), 457(44), 467, 462(59) Stull, D. R., 509(43), 557 Smith, T. D.S., 559(51), 550 Sturgeon, B., 352(64), 365(64), 390 Smucker, L., 52/(38), 404(32), 405(32), Subbarow, Y., 3(1), 4(1), 15 418(32), 428, 524(92), 538 Subramanian, S., 338(34), 389 Smyth, R. D. , 147( 1, 2) , 15 6(47), 164, Suckling, C. J , 558(46), 580 165, 296(2), 312 (73), 319, 322, 331 Sundaralingam, M., 65(55), 104 (9), 367(9), 388 Sutherland, I. O., 202(2), 204(2), 215 Sneeden, R. P. A., 559(56) (2) , 218(2, 55), 220(2, 55), 240, 242 Snook, G. F., 26(9), 102 Sutton, L. E., 338(30), 389 Sobel, H., 250(36), 288 Swallow, A. J., 318(96, 97), 319(97), Song, P. S., 422(101), 426(101), 430 525, 376(91, 92), 391 Songstad, J., 250(36), 288 Swanwick, M. G., 253(55), 288 Sorrell, T., 59(85), 85(85), 86(85), Sweany,R. L.,512(51),537 105 Swenson, C. A., 259(86), 306(55), 307 Spallo.C, 110(2), 120(2), 141, 152(26), (55), 310(55), 313(55), 522, 527(114), 154(26), 165 559, 549(15), 579 Sparks, R. A., 26(16, 17, 18), 40(16), Symons, M. C. R., 338(34), 559 103, 234(17), 240, 342(44), 389, 422 Szeverenyi, Z., 248(23), 252(47, 51,52), (100), 430, 467(9), 472(9), 482(9), 253(23,47), 257, 255 498 Spears, C, 156(51), 166, 250(33), 287 Tachkova, E. M., 255(78), 259, 513(58), Sperati, C. R., 404(35), 406(54), 418 557 (35), 428 Tackett, S. L., 252(41), 254(41), 255, Spiller, R. C., 24(3), 25(3), 102 418(88), 419(88), 430 Spiro, T. G., 343(56, 57), 344(56), 390 Tada,M., 317(89), 525 Sprinson, D. B., 149(16), 164 Taft, R. W., 259(84) Srivastava, R. C, 438(12a), 461 Tait, A. M., 250(32), 257 Stadlbauer, E. A., 527(116), 539 Takach,N. E., 706(118) Stadtman, E. R., 151(20), 165, 532(139, Takahashi, K., 150(19), 161(91), 764 140), 540 Takahashi, T., 115(19), 133(19), 742 Stadtman, T. C, 147(8), 155(8), 164, Takeuchi, S., 89(115), 106 528(120, 121), 529(120), 539, 574 Tamao, Y., 451(40), 462 (80), 581 Tanchiang, Y.-T., 497(52), 500 Stafford, W. S., 230(79), 234(79), 242 Tani, M. E. V., 706(110) Stahlberg, K.-G., 147(6), 164 Tanzher,G., 317(90), 525 Steen, V. D., 156(53), 166 Taube, R., 335(18), 559 Steeples, I. P., 285(204), 286(204), 294 Tauzher, G., 256(91), 270(91), 277(171), Stefani, L., 256(91), 270(91), 277(170, 280(91), 290, 292, 336(24), 559, 502 171), 280(91), 290, 292, 336(24), 389, (3) , 514(3), 555 502(3), 514(3), 535 Taylor, L. T., 252(40), 255 Steggles, P. N , 525(100), 526(100), 539 Taylor, R., 706(117), 266(106, 107), Stephens, R. S., 559(104) 290 Stephenson, G. F., 125(50), 143, 204 Taylor, R. T., 162(73, 74), 766, 527(38), (13), 240 404(32), 405(32), 418(32), 425, 524 Stephenson, J. R., 112(14), 113(14), (92), 528(122, 123), 555, 540 H4(14b),742 Taylor, S. E., 468(12), 499 Sternlicht, H., 489(42), 500 Tezuka,M., 300(17), 520 Stoeckli-Evans, H., 33(38), 103, 223(67), Thachuck, R. D., 482(24), 487(24), 488 224(67), 242, 342(46), 390 (24), 489(24), 493(24), 497(24), Stothers, J. B., 144(63) 499 Stotter, D. A., 266(106, 107), 290, 539 Thomas, R., 125(50), 744, 222(66), 242

Thompson, M., 122(43), 123(43), 125 Trkula,M., 85(89), 105 (43, 51), 126(51, 53), 129(43, 56), Trotman-Dickenson, A. F., 531(133), 130(56), 132(60), 133(60), 135(43, 540 60), 143,144 Trueblood, K. N., 26(12, 15, 16, 17, 18, Thomson, A. J., 401(17), 402(17), 403 20), 28(26), 40(16), 102, 103,106 (17), 422(17), 426(17), 427 (121), 110(7), 747, 202(1), 204(1, 10), Thornton, J., 456(5), 467(5, 7), 468(7), 205(16), 234(17), 240, 342(44), 389, 469(7), 471(7), 472(7), 473(5, 7), 482 422(100), 430, 467(9), 472(9), 482 (7) , 483(7), 484(7), 492(7), 493(7), (9), 498 494(7), 496(5), 498 Tsou, D., 512(52), 537 Thorp, R. G , 255(81), 289, 329(1), 333 Tucker, S. P., 270(144), 271(144), 275 (I) , 336(27), 343(52), 346(52), 347 (144), 297 (52), 348(52), 349(52), 350(52), 351 Turner, A. M., 456(5), 467(5, 7), 468 (52), 354(52), 362(52), 369(52), 388, (7), 469(7), 471(7), 472(7), 473(5, 7), 389, 390, 397(8), 404(22, 27, 28), 408 482(7), 483(7), 484(7), 492(7), 493 (8) , 409(8), 412(27, 67), 427, 429, 468 (7), 494(7), 496(5), 498

(10) , 482(29), 484(29), 487(29), 488 Tyagi,S., 485(34), 499 (29), 490(29), 491(29), 498, 499 Tinker, H. B., 518(77), 538 Udenfriend, S., 426(106), 430 Titchmarsh, D. M., 256(93), 257(93), Ueda,T., 300(17), 320 261(93), 263(93), 265(93), 266(108), Ugi, I., 255(76), 261(76), 289, 523(87), 267(108), 290 538 Tkachuck,R. D., 268(126), 291 Umani-Ronchi, A , 377(96), 597, 545 Tobe, M. L., 256(90>, 289 (4) , 558( 4), 57 7(4), 578 Todd, A. R., 110(5,7), 120(5), Umetani,T., 311( 65), 52 2 141, 202(2), 204(2, 11), 215(2, Umrikhina, A. V., 121(42), 122(42), 11), 218(2, 55), 220(11,55), 225 745 (II) , 226(11), 227(11), 230(79), Urry,W. H.,540 231(11), 234(79), 236(11), 238 Ushio, K., 306(51), 527 (11) , 240, 242, 417(81), 418(80), 429 Valiant, J., 26(8), 102 Tom, G., 517(75), 538 Valinsky, J., 68(57), 104, 461(29), 545 Toohey, J. I., 147(2), 156(47), 164, (5) , 578 165, 207(23), 211(23), 240, 306 Valinsky, J. E., 382(121), 592, 451 (36, (52), 321, 397(7), 401(7, 16), 403 37), 462, 547(6), 558(47), 559(47), (7), 405(7), 422(7, 16), 427 578, 580 Topich, J., 515(70), 516(70), 517(69), van den Bergen, A., 525(96), 539 535(70), 538 van den Broek, P., 245(100) Toraya, T., 65(56), 104, 306(51), 321, Vanngard,T., 437(11), 467 579(11) Vanston, N. J., 314(78), 522, 412(71), Toscano, P. G., 85(87), 705 429 Toscano, P. J., 86(95), 105, 359(72), 375 Van Voert, H. C, 409(62), 429 (72), 382(72), 597, 505(18, 20), 506 Veer,W. L. C, 404(44), 428 (20), 531(18, 20), 536 Veillard, A., 396(4), 398(4, 15), 400 Townscnd,C. A., 112(13), 113(16), 115 (15), 411(15), 419(15), 427, 530(131), (7), 117(26), 120(26), 142, 218(52), 540, 556(38), 562(38), 564(38), 576 241, 473(19), 479(19), 480(19), 481 (38), 579 (19), 499 Venerable, G. D., 253(54), 288, 506(23), Toxano, P., 491(47), 500 514(23), 536 Toy, A. D., 438(126), 461 Venkatesan, K., 33(36, 37), 103, 205(15), Trimm, D. L., 428 207(15), 240, 342(47), 344(47), 347 Trivedi, B. K. , 377(99), 37 9(99), 392, (47), 390 567(62), 580 Verenikina, S. G., 267(109, 110), 290

Vergamini, P. J., 301(24), 304(24), 320, Waters, J. M., 33(34), 103, 33(34), 78 354(70), 391, 404(31), 418(31), 428, (12), 103, 105 492(46),500, 552(20),579 Waters, T. N., 78(72), 105 Vickery, T. M., 258(96), 282(191), 293, Waters, T. N. M., 33(34), 103 297(5), 307(5), 316(86), 320, 323, Watson, C. J., 116(23), 142 575(88), 581 Watson, W. P., 284(198), 293, 532(136, Viennet, R., 420(99), 430 137, 138), 534(149), 540, 541, 571 Vitols, E., 159(62, 63), 161(63), 166, (73), 572(74), 575(73, 75), 581 449(34), 461 Weber, H., 144(10) Vitols, V. S., 163(82), 167 Weber, J. H., 262(103), 263(103), 290, Vlcek, A. A., 252(48), 288, 335(15), 525(93), 527(113), 538, 539, 571(70), 389 581 Vogelman, H., 110(2), 120(2), Webster, J. R., 567(59), 580 141 Weijel,M., 428(49) Vogelmann, H., 230(82), 231 Weissbach, H., 147(1, 2), 156(44, 47, (82, 84, 89), 238(82), 243 49, 50), 159(49), 162(73, 74), 163 Volcani, B. E., 156(47), 165, 296(2), (50, 79, 84), 764, 765, 766(51), 767, 312(73), 319, 321 254(71), 289, 296(2), 312(73), 319, Volpin, M. E., 516(72,13), 538 321, 331(9), 367(9), 528(122, 123), von Deuten, K., 92(127), 106 540 von Schlingmann, G., 40(47), 104 Werthemann, L., 69(58, 59), 104, 236 (91), 243, 538 Wade, R. S., 522(86), 538 West, B. O., 525(96), 539 Wagner, F., 72(60, 61), 104, 110(2), 120 West, P. R., 573(79), 581 (2), 141, 148(14, 15), 151(21), 152(15, Westrum, E. F., 509(43), 537 25), 154(25), 155(15), 164, 165, 211 Weyhenmeyer, R., 110(3), 120(3), (29, 30), 216(42, 44, 46), 217(42, 48), 747 226(42, 44, 46), 230(82), 231(34, 83, White, H. A., 576(91), 582 89), 235(91), 238(82), 241, 243, 278 White, J. G., 26(11, 12, 15, 17, 18,20), (174), 292, 298(7), 320, 417(79), 429 28(25), 102, 103, 110(7), 747, 202(1), Wagner, H. A., 152(28), 765 204(1, 10), 205(16), 240, 342(44), Wahl, D., 235(91), 243 389, 422(100), 430, 467(9), 472(9), Walerych, W., 154(38, 39), 765(41), 230 482(9), 498 (81), 242 White, R.C., 426(105), 430 Walker, G. A., 157(57, 59), 158(57), 159 Whitear, B. R. D., 300(21), 303(21), 320, (62,63), 161(63), 766 335(22), 389, 404(34), 405(34), 418 Walker, T. E., 268(127, 128, 129), 297, (34), 428 313(76), 322, 478(21), 486(36), 488 Whitcsides, G. M., 260(99), 290 (21), 489(21), 490(21), 493(48), 495 Whitlock,H., 125(50), 143 (21, 51), 497(51), 499, 500 Whitman, P. J , 112(13), 742, 473(19), Walling, C, 532(134), 534(134), 540, 479(22), 480(19), 481(19), 499 556(44), 580 Wick, A., 247(39) Wallis,0. C, 576(91), 582 Widdowson, D. A., 317(91), 323 Walters, W. A., 252(55), 288 Wijmcnga, H. G., 404(44), 428 Waltzman, R., 280(180), 293 Wild, H., 202(5), 209(5), 212(5), 214 Wang, D. M., 575(90), 582 (5), 217(5), 227(5), 230(5), 240 Ward, B., 404(22), 427 Wilkinson, G., 276(160, 162), 292, 340 Ward, D., 281(185, 186), 293, 549(1 3), (40), 389 578 Williams, D. A., 260( 100), 290, 539 Watanabe, E., 246(4), 254(62), 255(62), Williams, D. C, 115(18), 116(25), 117 256(62), 257(62), 263(62), 265(62), (25, 31, 32, 33), 118(33), 120(25b), 286, 289 122(43), 123(43), 125(43), 129(43), Watenpaugh, K., 404(25), 427 135(43), 742,143

Williams, F. R., 255(82), 289, Wolf, D. E., 26(8), 102, 110(6), 141, 527(112), 539 239(104), 243 Williams, J. R., 404(22), 427 Wolfe, R. S., 303(35), 321,490(43), Williams, R. J. P., 255(81, 82), 500 289, 311(69), 312(69), 314 Wong, L. Y., 256(90), 264(105), 289, (78), 322, 336(27), 338(32), 339 290, 518(79), 538 (32), 343(52, 53), 345(59), 346 Wood, J. M., 291(119, 120), 298(10), (52), 347(52), 348(52), 349 303(35, 36), 30 7(59), 312( 70), 320, (52, 53), 350(52), 351(52, 59), 321, 322, 405(45), 428, 432(4), 449 353(59, 66, 67), 354(52), 362 ( 4 ) , 460, 469(15), 486( 35), 49 0(43, (52), 369(52), 389, 390, 391(75), 50), 495( 50), 49 7(50, 52) , 499, 500, 394(1), 395(1), 397(8), 404(28), 407 504(7), 517( 76), 526( 105), 52 8(7), (1), 408(8), 409(1, 8, 60, 61), 412(60, 529(105), 535, 538, 539 67, 71), 413(61), 415(61), 418(68, 85), Wood, T. R., 25(5), 102, 239(104), 420(1, 68), 422(1, 68), 427, 429, 430, 243 451(38), 452(38), 456(5, 6), 458(57), Woods, D. D., 147(5), 164, 529(124, 462, 464(2, 3, 4), 467(5, 7), 468(7, 125), 540 10, 11), 469(2, 7, 11), 471(3, 7), 472 Woodward, R. B., 169-200, 202(5), 209(5), (7), 473(5, 7), 482(7, 29), 483(7), 484 212(5), 214(5), 217(5), 227(5), 230(5), (3, 7, 29), 487(3, 29, 40), 488(29), 490 240, 498(53), 500 (2, 29, 50), 491(29), 492(7), 493(7), Worner,G., 117(30), 143 494(3, 7), 495(50), 496(5), 497(50), Wozniak, W., 343(56), 344(56), 390 498, 499, 500, 527(110,112), 539, Wurziger, H. K. W., 117(31, 32, 33), 118 558(48), 580 (33), 121(41), 143 Willis, B. T. M., 313(75), 322 Wilson, M. R., 156(47), 165 Ya Bykhovsky, V., 132(60), 133(60), Wilt, J. W., 379(110), 392, 556(35), 135(60), 144 579 Yacynych, A. M., 85(90), 105 Windgassen, R. J., 158(61), 166, 240, Yagen,B., 116(24), 142 247(8, 9), 250(30), 252(9), 253(30, Yakovlev, V. A., 267(116, 117), 285 56), 256(8, 88), 257(94, 95), 258(97), (117), 290 269(8), 283(88), 287, 288, 289, 290, Yakusheva, M. I., 267(111), 290 300(22), 301(22), 302(22, 31), 303 Yamada, R., 253(57), 268(124), 288, (22), 304(40), 307(58), 311(58, 66), 291, 301(25), 302(30), 311(65), 320, 312(58), 313(31), 314(31), 320, 321, 321, 322, 432(3), 433(3), 439(3), 441 322, 404(30), 418(30), 419(30, 95), (3), 442(3), 449(3), 460, 508(38), 522 427, 430, 507(33), 508(36), 518(78), (84), 524(38), 525(38), 536, 538 524(33, 36), 525(33), 527(115), 529 Yamaguchi, K., 556(39), 580 (115), 536, 538, 539 Yamano, Y., 406(55), 419(55), 428 Winficld, M. E., 277(167), 292, 432(2, Yavorskaya, A. N., 121(42), 122(42), 3), 433(2, 3, 9), 434(9), 437(9), 439 143 (3, 9, 21), 440(9), 441(3), 442(21), Yoshida, Z ., 246( 4), 254( 62), 255( 62), 443(3, 21), 444(21), 445(21), 449(3, 256(62), 257( 62), 263( 62), 265( 62), 21), 453(9), 457(9), 458(56), 460, 286, 289 461, 462 Yoshizawa, J., 295(181) Winnacker, E. L., 214(41), 241(39) Yurkevich, A. M., 255(78), 267(109, Wintner,C. E., 78(75), 105 110, 117), 282(189), 284(199, 200, Wise, I. J., 161(69, 70), 166 201, 202, 203), 285(117, 200, 202), Witkop, B., 228(70), 242 289, 290, 293, 294, 298(8, 12), 299 Witman,M., 525(93), 538 (12), 305(49, 50), 306(49, 50), 320, Witman, M. W., 527(113), 539 321, 363(80, 81), 391, 513(58), 537, Woggon, W.-D., 132(60), 133(60), 135 549(14), 5 7 3(77), 575(85), 5 78, (60, 66), 144 581

Subject Index

Abbreviations, nomenclature, 20 2-Acetoxyethyl(pyridine)cobaloxime, Absolute configuration: 13C-Iabelled, 534 3-episirohydrochlorin, 130 Acetylcobalamin: vitamin B 12, 28 alkali, vitamin B 12, 311 Acetaldehyde: reaction with hydroxylamine. 312 [2-2H,3H]acetaldehyde Acetylene: from ethanolamine, 558 addition to cobalt(I) complexes, e hanolamine, vitamin B 1 2 coenzyme 256 photolysis, 298 carbanion reaction with cobalt(III) 2-ethoxyethylamine, vitamin B12 coenzyme complexes, 279 photolysis, 298, 328 pentacyanocobaltate, reaction with, ethylene glycol: 276 pulse radiolysis, 574 Acetylglycobalamin, reaction with vitamin B 12 coenzyme photolysis, hydroxylamine, 312 298 Achlorohydria, 1 methyl(aquo)cobaloxime photolysis, Acid catalysis: ethylene glycol, 571 alkylcorrins, decomposition, 369 Acctamide side chain, vitamin B 12, 2-hydroxyethylcobaloxime, olefin 30 7r-complcxes, 575 Acetic acid, carbon dioxide reduction, phenacylcobalamin, olefin n-complexes, 528 575 Acetoin, vitamin B1 2 total synthesis, Acid catalyzed decomposition isopropyl- 172 cobalamin rate, 371 Acetone: Acid catalyzed rearrangement to 0-hydroxy- bis(salicylaldehyde)ethylenediimine- ft-propylpyridinatocobaloximc, cobalt(lII)(CH3OH),alkylation, |3-hydroxy-isopropy lpyridinato- 518 cobaloxime, 314 cobalt alkylation, 280 Acid catalyzed,electrophilicdecomposition: cobalt(III) complexes, alkylation, alkylcobalamins, 527 517 2-hydroxyethylcobaloximes, 518 photolysis, /3-hydroxypropylcobaloximes, Acid cleavage: 302 adenosylcobaloxime, 312 reaction with aquohydroxo Co(III), adenosylcorrinoids, 312 336 Coa-adenyl-Co|3adenosy lcobalamin, Acetonitrile formation, methylcobaloxime 312 and cyanide, 307 3-isoadenosylcobalamin, 312 2-Acetoxyalkylcobaloximes: Acid decomposition: conversion to: 2,3,dihydroxy-4-pentenal, vitamin B 12 2-alkoxyalkylcobaloximes, 575 coenzyme, 312 olefin 7r-complexes, 575 cobalt-carbon bond, vitamin B1 2 preparation, 284 coenzyme, 366

Acid decomposition (Cont'd) olefins, mechanism: b-ethoxyctIiy 1(pyridine) cobaloximc, cobaloximes, 264 ethylene, 313 cobalt(I) complexes, 265 ethylene, hydroxyethylcobalaniin, hydridocobalt complexes, 313 265 methoxyethylcobalamin, ethylene, hydridopentacyanocobalt, 313 263 Acid hydrolysis: unsaturated electrophiles, cobalt(I) nucleotide loop, 234 complexes, 256 vitamin B 12: Adenosine-5 -carboxaldehyde, 363 chromatography, 230 formation, 297 cobyrinic acid, 230, 232, 234 structure, 297

Acidity: Adenosine triphosphate, vitamin B12 hydridocobalt complexes, 253, coenzyme, biosynthesis,

506 vitamin B 1 2 523 hydridopentacyanocobalt, 252 Adenosylating enzyme: Schiff-base complexes, 506 metal ions, 161 vitamin B 1 2S, 253 nucleoside triphosphates, 160 Acrylate radical, vitamin B 12 coenzyme, Adenosylation: glutainate mutase, 571 C. tetanomorphnm, table, nucleoside Acrylonitrile: triphosphates, 160 addition to cobalt(I) complexes, corrin, 155

256 Adenosyl carbene, vitamin B1 2 coenzyme, olefin p-complexes, cobalt(I) complexes, 549

527 Adenosylcobalamin, see Vitamin B12 Activation, corrin ring, S-adenosyl- coenzyme methionine, 345 Adenosylcobalamin-agarose, affinity methionine synthetase, 162 chromatography, 268 Activation enthalpy: ara-Adenosylcobalamin, reac ion with homolytie cleavage, cobalt-carbon bond, cyanide, 306 511 L-Adenosylcobalamin, reaction with kine ics, cobalt-carbon bond, 5 1 1 cyanide, 306 1-phenylethylcobaloximes, axial ligands, Adenosylcobaloxime: role, 5 1 1 acid cleavage, 312 Active site thiol, vitamin B 12 coenzyme, reaction with, alkali, 307 enzymic reaction, 555 Adenosylcobinamide, 155 1-Adamanthyl( pyridine)cobaloxime, Adenosylcobyric acid, 155 preparation, 255 Adenosylcorrinoids, acid cleavage,

Addition of chlorine, vitamin B 12, 312 216 S-Adenosy homocysteine, 363 Addition of guanosine diphosphate, S-Adenosylmethionine: cobinamide phosphate, 151 activation, corrin ring, 345 Addition of lower base, cobalamins, methionine formation, 329 biosynthesis, 153 Coa-adenyl-Co/b-adenosy lcobalamin, Addition to: reaction with cyanide, 305 cobalt(l) complexes: Adenylcobamide, coordination chemistry, acetylene, 256 351

acrylonitrile, 256 AdoCbl, see Vitamin B 1 2 coenzyme alkynes, 256 Adocobalamin, see Vitamin B12 coenzyme mechanism, olefins, 262 Aerobaetcr acrogenes, cobalamin olefins, 256 biosynthesis, 160 3,3,3-trifluoropropyne, 257 Affinity chromatography: corrin, conjugated system, 238 adenosylcobalamin-agarose, 268

Affinity chromatography (Cont'd) diazoalkanes: corrin, 268 cobalt(III) complexes, 281 ribonucleotide reductase, 268 cobalt porphyrins, 281 Aggrega ion, cobalamins, 491 electron transfer, cobalt(I) complexes,

Air dried crystals, vitamin B 12, 259 25 gold(I), alkylcobalt complexes, Alkali: 527 adenosylcobaloxime, 307 Grignard reagent, cobalt(III) complexes, reaction wi h alkylocobalt complexes, 277,517 307-311 hydrazines and oxygen:

vitamin B 12, cobalt, reduction by, cobaloximes, 275 226 cobalt complexes, 275

vitamin B 12s, acetylcobalamin, kinetics, table: 311 cobaloximes, 259 Alkaline decomposition: cobalt(I) complexes, 258

cobalt-carbon bond, vitamin B12 mercury(II),

coenzyme, 366 vitamin B 12S, 259 cyanocthylcobalamin, 366 mercury(II), methylcobalamin, ethoxycarbonylcobalamin, 360 526 Alkaline phosphatase: metliylpentacyanocobaltate(III), mercuric cobalamin phosphate, dephosphoryla- chloride, 526 tion, E. coli, 155 nitromethane, cobalt, 280 2-Alkoxyalkylcobaloximes, 2-acetoxyalkyl- olefin addition: cobaloximes, conversion to, 575 cob(I)aloximes, 523 Alkylating agents, cobalt complexes, 254 cobalt(I) complexes, 523 Alkylation: organolithium reagents, cobalt(III) acetone, bis(salicylaldehyde)ethyIene- complexes, 517

diiminecobalt(III)(CH3 OH), 518 palladium(II), alkylcobalt complexes, cobalt(III) complexes, 517 527 alkyl halides: pentacyanocobaltate, 502 cob(I)aloximes, 523 platinum(IV), alkylcobalt complexes, cobalt(I) complexes, 523 527 cobalt(II) complexes, 518 radical intermediates: tricyclohexylphosphinecobal(II)oximes, bis(salicylaldehydc-o-phenylenediimine- 519 cobalt(II), 518 vitamin B 12r, 520 cobalt(II) complexes, 518

vitamin B 12s, 523 vitamin B 121 -, 520 alkyl iodides versus other alkyl halides, stereochemistry: cobalt(Il) complexes, 522 cob(I)aloximes, 523 alkylcobaloximes, mercury(ll), cobalt(I) complexes, 523

526 vitamin B 12S, 260, 523

alkylcobalt complexes: synthetic utility, vitamin B 121 -, arsenic(III), 526 277 mercury(II), 526 tin(IV), alkylcobalt complexes, thallium(III), 526 527 axial ligand effects, cob(II)aloxirnes, trans-dimethylcobalt(III) complexes: 519 cadmium, 527 cobalt(I) complexes, stereochemistry, lead(II), 527 vinyl halides, 260, 502 zinc(II), 527 cobalt(III) complexes, cobalt-carbon vinyl e hers: bond formation, 517-524 cob(III)aloxime, 281 corring, 214 hydroxocobalamin, 281 CoTPP, disproportionation, 279 Alkylcarbinylcobalamin, 362

Alkylcobalamins: halogen cleavage, 317 acid catalyzed electrophilic decomposi- heterolytic cleavage, 305-319 tion, 527 hexachloroiridate, oxidation, table, 516 alkyl reactions, 295-323 mercury(II), alkylation, 526 base-on, off, photolability, 303 oxidation, one electron, 515 bond dissociation energy, 513 photolysis: cobalt-carbon bond thermolysis, epr spectroscopy, 525 525 quantum yield, 300-303, 364, 525 conformations, 341 pyridine complexes, hydrolysis, 248 5- and 6-coordinate, 346, 351 reaction with mercaptides, 311 dealkylation by thiols, 527 redox chemistry, 515 c/s-diaminoplatinum(II) coordination, redox potential, 516 495 thermolysis, 303, 364 five coordinate, decomposition, 369 X-ray crystallographic data, 80 heterolytic cleavage, 305-319 X-ray structure, 359 13C-Iabelled, 268 see also Alkylcobalt complexes nomenclature, 21 (Alkylcobalt)+, nuclcophilic displacement, one-electron oxidation, 517 R+ from, 516 photolability, 524 Alkylcobalt complexes:

photolysis, role of, O2 , 366 alkylation:

vitamin B 128, formation, 300-303 gold(I),527 pK values, benzimidazole, table, 351, palladium(II), 527 494 platinum(IV), 527 protonation, table, 35 1 tin(IV), 527 quantum yield, photolysis, 303 alkyl reactions, 295-323 rate of decomposition, 365, table, 368 arsenic(III), alkylation, 526 reaction with: bond dissociation energy, Schiff-base acid, 313 complexes, 5 1 2 cyanide, 306 cobalt-carbon bond: steric effects: length, table, 505 ligand exchange, 341 thermolysis, 525 on structure, 341 flash photolysis, 525 thermolysis, 303 formal oxidation state, 514 thiols, 527 5,7,7,1 2,14,14-hcxamethyl-l,4,8,11- very strained, rate of decomposition, tetraazacyclotetradeca-4,11-dieneco- 371 balt, 271

vitamin B 12r, reductive cleavage, ligand modification, 283-286 317 mercury(Il): see also Alkylcobalt complexes; Cobalt alkylation, 526 complexes; Cobalt-carbon bond; stereochemistry, 526

Me hylcobalamin; VitaminB 12 model systems, vitamin B 12 coenzyme, coenzyme 551,564 Alkylcobaloximes: photolability, 553 alkyl ligand reactions, 295-323 photolysis: axial Ugand exchange rates, 248 anaerobic, 553 cation radicals, epr spectrum, 515, 517 bis(acetylacetone)ethylenednminecobalt, chromatography, 247 524 cobalt-carbon bond length, 359 bis(salicylaldehyde) ethylcnediimine- crystallization, 248 cobalt complexes, 524 dealkylation, thiols, 527 diacetylmonoximcimino diacetylmono- electrochemical oxidation, 515 ximatoiminopropane-1,3-cobalt(I), electronic spectrum, 406 524 b-elimination, 364 1,4,8,11-tetraazacyclotetradecane, 524

Alkylcobalt complexes (Cont'd) vitamin B 12r: quantum yield, 553 alkylation 520 radical traps, 553 reaction with 274

spin-traps, 524, 552 vitamin B 12S, alkylation, 523 reaction with tetracyanoethylene, 285 Alkyl iodides, cobalt(II) complexes, alkyla- redox chemistry, diacetylmonoximeimino tion, 522 diacetylmonoximatoiminopropane- Alkyl ligands: 1,3-cobalt, 514 cobaloximes, optically active, thallium(III) alkylation, 526 268 1,4,8,11-tetraazacyclotetradccane, 524 effect on physical properties, table, thermolysis, 552 corrin, 356 transalkylation, cobalt(I) complexes, 527 electronic spectrum, effect, 356 see also Cobalt-carbon bond pK values, effect, 356 Alkylcobalt(IV) complexes, SchifT-base reactions, 295-323 complexes, 516 Alkylperoxocobalt complexes, 55 3 Alkylcobinamides: Alkyl(pyridine)cobaloximes, cation ex- electronic spectrum, temperature varia- change resin, hydrolysis, 249 tion, 348 Alkyl radicals, cobalt, recombination with, pH decomposition rates, 370 335 Alkylcorrins: Alkyl reactions: cobinamides cobalamins, 369 alkylcobalamins, 295-323 decomposition, acid catalysis, 369 alkylcobalt complexes, 295-3 23 imidazole coordination, 358 Alkynes: olefins decomposition, 365 addition: photoaquation, 301 cobalt(I) complexes, 256 photolysis, olefins, 302 mechanism, 263 Alkyl halides: stereochemistry, 256 bis{ 1,2-cyclopentanedioximato) cobalt, Alkynylcobalt complexes, synthesis, 279 Amide activation, vitamin B , total synthe- cobalt(II) complexes, reaction with, 12 sis, 192 274 f-Amide cleavage, group participation bis(salicylaldehye-o-phenylenediimine- effects, 231 cobalt) Co, cobalt(II) complexes, Amide dcamination, vitamin B total reaction with, 274 12 synthesis, 191 cob(I)aloximes, alkylation, 523 Amide groups (corrin periphery): cobalt(I) complexes, alkylation, 523 hydrolysis: cobalt(II) complexes: acid, 230 alkylation, 518 base, 234 halogen abstraction, 519 rates of hydrolysis, steric, 231 reaction with, 273 vitamin B 12 hydrolysis, side chain, reactivity towards, 521 33 pentacyanocobaltate: Amide hydrolysis, dinitrogen tctroxide. olefins from 519 VitaminB12 total synthesis, 192 reaction with 274 Amide side chain, nomenclature, vitamin

reactivity towards: B 12, 19,30 bis(salicylaldehyde-o-pheny lenediimine- Aminoalcohols (vicinal), radical rearrange- cobalt(II) (py), 521 ments to aldehydes, 573 pentacyanocobaltate, 521 Aminocobalamin, electronic spectrum, triphenylphosphine cob(II)aloximes, 521 411 vitamin B , 521 12r 10-Aminocabalamin,217 1,4,8,1 1-tetraazacyclotetradecane: 8-Aminocobyrinic acid abcdefg-hexamcthyl cobalt(II), reaction with, 274 ester c-lactam, preparation, 236 tricyclohcxylphosphinecobal(II)oxime, alkylation, 519

8-Aminocobyrinic acid c-lactam dicyanide, Apoenzyme, circular dichroism, binding of see Hcxacarboxylic acid, vitamin B12 corrin, 423 /3-Aminoethylcobalt complexes, preparation, Coa-aquo-Co/3-adenosylcobamide, reaction 257 with cyanide, 306 2-Amino-2-hydroxy radical, 558 Aquocobalamin, 5-Aminolevulinic acid, incorporation into, circular dichroism, 420 corrin, 111 electronic spectrum, 417 13 [5- C]-aminolevulinic acid, vitamin B 1 2, enzymic reduction, 157 biosynthesis, 479 ligand substitution, equilibrium constants,

2-Aminomebularine, vitamin B12 coenzyme, table, 337 fluorescent analogs, 300 nmr spectrum, praseodymium, 468, 474, Aminome hylbilanes: 483 corrin biosynthesis, 117 pulse radiolysis, 318 deamination, 118 reaction with: porphobilinogen deaminase, deamination, malononitrile, 279 117 phenylacetonitrile, 279 structure, 11 8 redox potential 5 14 Aminomutases: see also Cobalt complexes; Hydroxo- enzymic reaction, 546 cobalamin MO calculations, 557 Aquocob(II) inamide:

model systems, vitamin B12 coenzyme, epr spectrum, 448 571 Aquocyanocobinamide, electronic spectrum, pyridoxal phosphate, 329 408, 413 radical intermediates, 556 Aquocyanocobyric acid: reaction pathways, vitamin B 12 coenzyme, bond lengths, 206 573 structure, 205 2-Amino-l-propanol, radical intermediates, Aquohydroxo Co(III): enzymic reaction, 450 acetone, reaction with, 336 [R] -l-Amino-2-propanol: nitromethane, reaction with, 336 nucleotide loop, biosynthesis, 149 Aquohydroxocobinamide, electronic- phosphorylation, 151 spectrum, 413 synthesis, 1 3 Aristeromycyclocobalamin : L-threonine, conversion to, 199 photolysis, 297 threonine decarboxylation, 150 reaction with: Anaerobic photolysis, alkylcobalt com- cyanide, 306 plexes, 55 3 hydroxide, 307

Analogs, vitamin B 12 coenzyme, 551 Arndt-Fistert, vitamin B 12 total synthesis, Analysis of reaction mixtures, cobalt- 194 carbon bond synthesis, 247 Aromaticity: [14] Ane HA, see 1,4,8,11-Tetraaza- corrin, 204

cyclotetradecane vitamin B12 204 Angular anomalies, cob(II) inamides, epr Arsenic(IH) alkylation, alkylcobalt com- spectroscopy, 443 plexes, 526 4',5'-Anhydroadenosine, 549 Arylcobaloximes, 271

Animal protein factor, vitamin B12, 14 Aryl cobalt complexes, bis(acetylacctonc) m-Anisidine, vitamin B 12 total synthesis, ethylenediiminecobalt, 275

172 Aryl halides, vitamin B 12s , reaction with, Anisotropic hyperfine interaction, cob(Il) 271 inamides, epr spectroscopy, 443 10-Aryloxycobalamin, 217 Anomalous dispersion. X-ray structure, Ascorbic acid: role in formation, yellow corrinoids, 39 97 vitamin B 12, reaction with, 229 Antipernicious anemia factor, vitamin B 12, yellow corrinoids, 229 11

Assay, vitamin B 12 coenzyme, biosynthesis, Benzylcobalamin, stability, 255, 513 vitamin B 12S, 159 Benzylcobaloxime, halogen cleavage, 317 Atrophic gastris, 1 Benzylcobalt complexes, thermal stability, Axial ligand effects, cob(H)aloximes, alkyla- 513 ion, 518 Benzylcobalt(octaethylporphyrin), stability, Axial ligand exchange rates, alky lcobal- 255 oximes, 248 Bilanes: Axial ligands: aminomethyl: cobalt-carbon bond, bond dissociation corrin biosyn hesis, 117 energy, 531 deamination, 118 equilibria, 345 hydroxymethyl, corrin biosynthesis, role, activation enthalpy, 1-phenylenthyl- 118 (pyridine)cobaloxime, bond dis- 1-methyl, corrin biosynthesis, 121 asssociation energy, 510 Binding of corrin to apoenzyme, circular steric requirements, corrin, 255 dichroism, 423 vitamin B12 coenzyme constraint of, 41 Binding to apoenzyme, side chain modifica- 5- and 6-coordinate corrin, 346 tion, 65 Axial phosphincs bond lengths, cobaloximcs, Binding to ribonucleotide reductase, 83 B nr , 442 Azidocobalamin, electronic spectrum, 411, Biological activity: 417 lactams (corrin ring), 225 Azidocob(ll)inamide, epr spectrum simula- neocorrinoids, 8-epicorrinoids, 225 ion, 445 neovitamin B12, 224 Biosynthesis: B coenzyme, see Vitamin B coenzyme 12 12 addition of lower base, cobalamins, B , see Vitamin B 12r 12r 153 B see Vitamin B 12 s> 12 s Aerobaeter aerogenes, cobalamins, 160 7-Band, electronic spectrum, effect of [5-13CJ 5-aminolevulinic acid, vitamin axial ligands, 411, table B 12, 479 Base-on, off: [R]-l-amino-2-propanol, nucleotide electronic spectrum, vitamin B 12 loop, 149 coenzyme, 357 Clostridium stieklandii, cobalamins, epr spectrum, vitamin B -, 299 121 153 isopropylcobalamin, thermolysis, 552 Clostridium thcrmoaceticum, methyl- photolability, alkylcobalai.iins, 303 cobalamin, 161 vitamin B coenzyme, 350 12 cobalamins: Beckmann rearrangement, vitamin B 12 from cobyric acid, 148 total synthesis, 180 nucleotide loop, 148 Benzimidazole: cobinamides, 151, 152 alkylcobalamins, pK values, 351 corrin, nucleotide loop, 107-144, 148 effect on corrin ring folding, 59 E. eoli, metliylcobalamin, 161 pKa values when coordinated, 54 Euglena gracilis, corrin, 117 vitamin B 12 coenzyme pK values, eukaryotes: 351 cobalt-carbon bond, 155 /V-Benzoyladenosylcobalamin, reaction with vitamin B 12 coenzyme, 156 cyanide, 306 Factor I, 131 Benzoyl! 1-pyridine) methanide(chloro)- FMNH 2 : cobaloxime, preparation, 276 cobalamins, 148 Benzyl bromide: methionine, 162 reaction with: guanosinc diphosphate, nucleotide loop, 152 vitamin B , 5 1 3 12 r L. leichmannii, cobalamins, 160 vitamin B , 51 3 12 s Methanosarcina barkeri, metliylcobalamin, Benzylaquocobaloximc, redox potential, 516 162

Biosynthesis (Cont'd) pKa values, 504 l 3 [ CH 3 ]-L-methionine, vitamin B12, 480 l,l-Bis-(p-chlorophenyl)-2,2,2-trichloro- 1-methylbilane, corrin, 121 ethane, reaction with methy lcobalamin: cob(I)aloxime, 266 mammalian, 163 Bis(l,2-cyclopentanedioximato) cobalt: methane, 161-163, 528 cobalt(II) complexes, reac ion with alkyl NADPH: halides, 274 me hionine, 162 nucleophilicity, cobalt(I), 251 methy lcobalamin, 162 Bis(dimethylglyoximato) cobalt, see Cobaloximes nicotinate mononucleotides, cobalamins, Bislactone, sirohydrochlorin, 122 153 Bis(salicylaldehyde)ethylenediimine-

nmr spectroscopy, vitamin B 12, 479 cobalt(II)(methylimidazole): origin of carbon atoms, cobyrinic acid, halogen abstraction, electron transfer, 112 520 5-phosphoribosyl-l-pyrophosphate, six coordinate, 519 cobalamins, 153 Bis(salicylaldehyde)ethylenediimine- 1 3 [8- C] porphobilinogen, vitamin B12 , cobalt(III): 480 alkyl complexes, photolysis, 524 primary precursors, cobyrinic acid, 112 methyl complex, photolysis, 301 prokaryotes: model systems, vitamin B12 coenzyme, cobalt-carbon bond, 155 551

vitamin B 12 coenzyme, 156 nucleophilicity, 523 Propionibacterium arabinosum, nucleotide propyl complex, photolysis, 302 loop, 152 reaction with carbanions, 279 Propionibacterium shermanii, corrin, redox potential, bis(acetylacetone)- 112 ethylenediiminecobalt, 504 ribose-l-phosphate, cobalamins, 153 structure, 552 sirohydrochlorin, 123 vitamin B 12 coenzyme, model systems, Streptomyces griseus, methylcobalamin, 551 161 7,7 '(CH 3 )2 bis(salicylaldehyde)ethylene- timing, cobalt-carbon bond formation, diiminecobalt, pKa values, 504 155 Bis(salicylaldehyde-o-phenylenediimine)- trimethylated i sobacteriochlorins, 132 cobalt, pKa values, 504 uroporphyrinogen(III) as precursor of Bis(salicylaldehyde-o-phenylenediimine- cobyrinic acid, 116 cobalt(II)(py): alkylation, radical intermediates, 518 VitaminB12 coenzyme, 145-167 alkyl halides, reactivity towards, 521 VitaminB12, 28, 107 Bis(salicylaldehyde-o-phenylenediimine)- vitamin B 12s: cobalt(III): adenosine triphosphate, vitamin B12 cobalt(II) complexes reaction wi h alkyl coenzyme, 523 halides, 274 assay, vitamin B 12 coenzyme, 159 redox potential, 504 Biosynthetic studies, nmr spectroscopy, structure, 503 486 Bond angles, distances, corrins, tables, Bis(acetylacetone)ethylenediamine, X-ray 45-53 structure, complex with methyl- Bond dissociation energy: cobalamin, 349 alkylcobalamins, 513 Bis(acetylacetone)e hylenediimine- axial ligands: cobalt(III), structure, 503 cobalt-carbon bond, 531 Bis(acetylacetone)ethylenediiminecobalt: role, l-phenylethyl(pyridine)- alkyl complexes, photolysis, 524 cobaloxime, 510 aryl cobalt complexes, 275 cobalt-carbon bond, steric effects, 507, 512 bis(salicylaldehyde)ethylenediimine- cobalt, redox potential, 504

Bond dissociation energy (Cont'd) methyl(triphenylphosphine)cobaloxime, conforma ional changes, cobalt-carbon cobalt-carbon bond, 505 bond,531 nmr spectroscopy, methylcobalt complexes, 1-cyanoethylcobaloxime, cobalt-carbon 506 bond,511 observed and ca lculated, corrin, 205, equilibrium determination, 1-phenylethyl- table, 206 (pyridine)cobaloxime, 508 vinyl(pyridine)bis(salicylaldehyde)- hydridocobalamin, 507 ethylenediiminecobalt, co balt- hydridocobalt complexes, 506 carbon bond,505 hydridopentacyanocobalt, 507 vinyl(pyridine)cobaloxime, cobalt- hydrido(pyridine)cobaloxime, 507 carbon bond,505

hydrido( tri-w -b uty lphosphinc) cobaloxime, vitamin B 12 coenzyme, cobalt-carbon 507 bond,505 isopropylcobaloxime, cobalt-carbon bond, s-Bonded organocorrinoids, vitamin B 12 511 sscoenzyme, enzymic reactions, isopropyl(pyridine)bis(salicylaldehyde-o- sss547

phenylenediimine)cobalt, 512 p-Bonding, vitamin B 12r, 440

1-methyl-heptylcobaloxime,cobalt- Bond strength, vitamin B 12 coenzyme, carbon bond,511 cobalt-carbon bond, 513 l-methyl-2-phenylethylcobaloxime, Borohydride cleavage, carboxymethyl- cobalt-carbon bond, 511 cobalamin, 303 neopentyl(pyridinc)bis(salicylaldehyde-o- Bridged cation: phenylenediimine)cobalt, 512 diol dehydrase, enzymic reaction, 555 propyl(pyridine)bis(salicylaldehyde-o- molecular orbitals, 555 phenylenediimine)cobalt, 512 theoretical studies, 557 Schiff-base complexes, alkylcobalt com- Bridged cobaloximes, structure, 87, plexes, 512 269 steric effects, cobalt-carbon bond, 512, Bridged dimers, cobaloximes, 268 531 Broken cell enzymes, corrin bio-

vitamin B12 coenzyme, cobalt-carbon synthesis, 116 bond, factors affecting, 531 Bromination: Bond leng hs: corrin, 215

aquocyanocobyric acid, 206 vitamin B12, 215 cobaloximes, axial phosphincs, 83 1 0-Bromocobalamin: cobalt-carbon bond, steric crowding, 505 acetylcobalamin, 411 corrin, table, 48, 49 axial ligands, table, 414, 415 15-cyano-l,2,2,7,7,12,12-heptamethyl- chlorocobalamin, 411 corrin, 206 preparation, 216 isopropyl(pyridinc) cobaloxime, cobalt- 3-Bromopropylcobaloxime, thermolysis, carbon bond,505 304 isopropyl(tricyclohexylphosphine)- Buckling: cobaloximc, cobalt-carbon bond, corrin, 208, 342 506 vitamin B12, 208 isopropyl(triphenylphosphine)- But-3-enylcobalamin, cyclopropyl- cobaloxime, cobalt-carbon bond, carbinylcobalamin, rearrange- 505 ments, 567 methyl(aquo)cobaloxime, cobalt-carbon But-3-enyl(pyridine)cobaloxime, cyclo- bond,505 propylcarbinyl(pyridine) cobal- methyl(pyridine)bis(acetylacetone)- oxime, rearrangements, 568 ethylenediiminecobalt,cobalt- But-3-enyl radical: carbon bond,505 cyclopropylcarbinyl radical rearrangements methyl(pyridine)cobaloxime,obalt- 557 carbon bond, 505 t-Butylcobaloximes, 254

13 C, biosynthetic studies: Carbon-skeleton rearrangements: dicyanocobalamin, nmr spectrum, 112 epr spectroscopy, 381

vitamin B 12, nmr spectrum, 112, 480 mechanism, 385 C-12, first step in corrin biosynthesis, protein-free models, 377 decarboxylation, 120 rearrangements, role of cobalt-carbon

C-13 epimer, neovitamin B 12 , 33 ntermediate, 382

C-Iactone structure, vitamin B12, 227 Carbonylcobaloxime, 309 C. tetanomorphum: Carboxylatopentaaminecobalt(III) Factor I, isolation from, 130 omplexes, photolysis, 272 nucleoside triphosphates, adenosyla- Carboxylic acids: tion, 160 corrin oxidation, 218

sirohydrochlorin, incorporation into, preparation, vitamin B12 , 231 123 Carboxymethylcellulose, corrin Cadmium: chromatography, 249 alkylation, trans-dimethylcobalt(III) Carboxymethylcobalamin: complexes, 527 borohydride cleavage, 303 incorporation into 15-cyano-l,2,2,7,7,12, lanthanide shift reagents, nmr spectrum, 12-heptame hylcorrin, 211 472

Calcula ions, vitamin B 12 coenzyme, elec- photolysis, 302 tronic spectrum, 398 pKa values, 316 (+)Camphor: spin-lattice relaxation imes, 492 conversion to c/s-isoketipinic acid, 174 Carboxymethylcobaloxime, thermolysis,

ring C, vitamin B12 total synthesis, 184 304

vitamin B12 total synthesis, 174, 193 Carboxymethylcyanocobalamin, Camphorquinone: electronic spectrum, 413

vitamin B12 total synthesis, 183 15-Carboxy-15-norcobinamide: Canonical resonance structures: decarboxylation, 239 corrin, 205 preparation, 239

vitamin B12, 205 vitamin B12, conversion to, 239 Capped cobaloximes: Catalysis, sodium borohydride reduction,

model systems, vitamin B12 coenzyme, cobalt complexes, 252 533,565 Catalytic reduction, nickel 1,19-dimethyl- structure, 269, 533, 565 octadehydrocorrin, 238 Carbanion intermediates, methylmalonyl- Cation exchange resin, hydrolysis, alkyl- CoA mutase, 556 (pyridine)cobaloximes, 249 Carbanions: Cation radicals: bis(salicylaldehyde)ethylenediimine- alkylcobaloximes, 515,517 cobalt(III), reaction with, 279 epr spectrum, alkylcobaloximes, 517 cobalt(III) complexes, reaction with, Cba, see Cobamides 279 Cbi, see Cobinamides Carbenes, reaction with cobalt(III) Cbl, see Cobalamins complexes, 279 Cby, see Cobyric acid p-Carbomethoxyphenylcobinamide, CD, see Circular dichroism preparation, 271 Cell dimensions, corrin derivatives, 92-97 Carbon dioxide, reduction to, acetic acid, Cell free enzymes, corrin biosynthesis, methylcobalamin, 528 116 Carbonium ion mechanism, isomerase Cerium(III) hydroxide, cobinamide from

reactions, 377 vitamin B 12, 236 Carbon monoxide: Charge-transfer: cobalt-carbon bond, reductive cobaloximes, electronic spectrum, 419 cleavage, 515 corrin, 403 oxidation, cobalt(III) complexes, electronic spectrum, cobalt-carbon bond, 515 394,403

Chemical degradation, vitamin B12, 111 CIDNP measurements, radical pair recom- Chemical formulae, corrin derivatives, bination, 512 92-97 Cinnamyl(imidazole)cobaloxime, reaction Chemical shifts (nmr): with tetracyanoethylene, 286

vitamin B 12 coenzyme, 465, 470 Circular dichroism:

vitamin B 12/, 485 aquocobalamin, 420

vitamin B 12,485 binding of corrin to apoenzyme, 423 Chemical synthesis: cobalt-free corrin, 421 cobinamides, 152 cobinamides, 421

vitamin B 12, 172-197 cobyric acid, 421 Chirality: corrin: corrin, 209 pentadecaalkyl from, 237

vitamin B 12, 170 sign inversion, 420-426 Chiral methyl, methionine, 115 dicyanocobinamide, 421, 424 Chiroptic effects, corrin, 207 a, b-isomers, corrin, 421 Chloramine T reaction with: methylcobalamin, 420 corrin, 215 neocorrinoids, 8-epicorrinoids, 222,

vitamin B 12, 215 225 Chlorination: protein bound, 426

dehydrovitamin B 12, 215 sirohydrochlorin, 122

electronic spectrum, vitamin B12, 215 tetracarboxylic acid, 421 vitamin B 12, 215 vitaminB12 , 223,420 l-Chloro-2,2-^/s(/?-chlorophenyl)ethyl- vitaminB12 coenzyme, 421 cobalamin: cis-Effect: trans-4,4 -dichloros ilbene, decomposi- cobaloximes, 85 tion, 304 corrin, 330 Chlorocobalamin, 411 nmr spectroscopy:

10-Chlorodehydrovitamin B12: cobalt complexes, 487 electronic spectrum, 215 corrin, 487 preparation, 215 vitamin B12 halogenation, 216 Chloromethylcobalamin, photolysis, 303 cis-Isoketipinic acid, (+)camphor conversion Chloromethylcobaloxime, thermolysis, to,174 304 Claisen rearrangement, amidoacetal,

Chlorosulfonyl isocyanate, cyanation of vitamin B12 total synthesis, corrin, 213 184 Chromatography: Cleavage: acid hydrolysis products, vitamin B12, cobalt-carbon bond: 230 photolytic, 524

alkylcobaloximes, 247 vitamin B 12 coenzyme, 547-554 carboxymethylcellulose, corrin, 249 electrophilic, cobalt-carbon bond, cobaloximes, 247 526 corrin, ion exchange, 247, 249 energetics, cobalt-carbon bond, 551 DEAE cellulose, corrin, 249 halogens, cobalt-carbon bond, 516, 526 neocorrinoids, 222 homolytic, cobalt-carbon bond, 524

phosphocellulose, corrin, 249 induc ion, vitamin B12 coenzyme, cobalt- separation of neo and normal corrins, carbon bond,550 222 mercury(II), cobalt-carbon bond, 526 sephadex, corrin , 249 methylcobalamin, iodine, 316 Chromic acid oxidation: models, cobalt-carbon bond, 88 dehydrocobinamide, 226 modified cobalamins, cobalt-carbon bond,

vitamin B 12, 218 65 Chromium(II), cobalt complexes, reduction, nucleophilic attack, cobalt-carbon bond, 254 527

Cleavage (Cont'd) trifluoromethylcobaloxime, reaction radical transfer, cobalt-carbon bond, 526 wi h hydroxide, 309 stereochemistry, (S)-methylheptyl- Cob(I)inamide: pyridinatocobaloxime, iodine, electronic spectrum, 419 317 nucleophilicity, 250, 251 thallium(III), cobalt-carbon bond, 526 see also Vitamin B 128

vitamin B 12 coenzyme, iodine, 316 Cob(II)alamin, see Vitamin B 121 . Clostridium sticklandii, cobalamins, bio- methyl radicals, recombination, 511 synthesis, 153 Cob(II) aloximes: Clostridium teta nomorphum, source o f alkylation, axial ligand effects, 519 corrin, 146 dispropor ionation, 253 Clostridium thermoaceticum, methyl- photolysis, methylcobaloxime, 301 cobalamin biosynthesis, 161 reaction with:

CMS, see Vitamin B12 carboxylic acids equilibrium data, 504 Coa-aquo-Cob-adenosyl(3,5,6-trimethyl- kinetics, 504 benzimidazolecobamide), reaction 1-phenylethylcobaloximes, 504 with cyanide, 306 Cob(II)amides: Coa-cyano-Co/3-alkylcobamides preparation, epr spectrum simulation, table, 446 307 fifth axial ligands, epr parameters, table, Coa-[a-(5,6-dimethylbenzimidazolyl] - 444 Co/3-adenosylcobamide, see Cob(II)inamides:

Vitamin B 12 coenzyme electronic spectrum, 418 Coa-[ a-(5,6-dimethylbenzimidazolyl ]- epr spectroscopy: Cob-(5-deoxy-5-adenosyl)cobamide, angular anomalies, 443

see Vitamin B12 coenzyme anisotropic hyperfine interaction, Co(BAE), see bis{Acetylacetone)ethylene- 443 diiminecobalt; Cobalt complexes function of fifth ligand, table, 444 Co(cHx2H2),see bis(l,2-Cyclohexane- epr spectrum, high pH, 434, table, 447 dionedioximato) cobalt; Cobalt magnetic circular dichroism, 426 complexes oxygenation, epr spectrum, 458 Co(cP2H2),see bis(l,2-Cyclopentane- Cobalamin auxotrophs, 163 dioximato) cobalt; Cobalt complexes Cobalamin coenzymes, interconversion,

Co(D2B2F4),see Cobaloxime-BF2 bridged; 163 Cobalt complexes Cobalamin phosphate, dephosphorylation, Co(D2H2),see Cobaloxime; Cobalt com- E. coli alkaline phosphatase, 155 plexes Cobalamin reductases, 158 Co(SALEN), see Ms(Salicylaldehyde)- Cobalamins: e hylenediiminecobalt; Cobalt aggregation, 491 complexes alkylcorrins vs. cobinamides, 369 Co(SALOPH), see bis(Salicylaldehyde-o- biosynthesis: phenylenediiminecobalt; Cobalt addition of lower base, 153 complexes Aerobacter aerogenes, 160

Cob(I)alamin, see Vitamin B 128 Clostridium sticklandii, 153 Cob(I)aloxime: from cobyric acid, 148 alkylation: L. Ieichmannii, 160 alkyl halides, 523 nicotinate mononucleotides, 153 olefin addi ion, 523 5-phosphoribosyl-l-pyrophosphate, stereochemistry, 523 153 l,l-Ms-(p-chlorophenyl)-2,2,2-trichloro- ribose-l-phosphate, 153 ethane, reaction with, 266 bound to human intrinsic factor, table, 2-hydroxyethylcobaloxime, reaction electronic spectrum, 417 with alkali, 310 cobyric acid, conversion to, 148 nucleophilicity, 523 configurations, N-glycosides, 153

Cobalamins (Cont'd) nmr spectrum, 247

conversion to vitamin B 12 coenzyme, nucleophilicity, cobalt(I) complexes, 156 251 coordination, mercury(II), 495 optically active, alkyl ligands, 268 correlation between nmr and electronic photolysis, 419 spectrum, 418 planarity deviations, 505 deficiency, 157 reduction, sodium borohydride, 251 as-diaminoplatinum(II) coordination, reductive alkylation, 248 495 steric effects, 86 electron (hydrated), 254 structure, 246 FAD, 157 ter iary alkyl, 254 FMN, 157 fraws-effect, table, 82 NADH, 157 X-ray crystallographic data, 80-90 epr comparison to cobinamides, 448 X-ray crystallography, vitamin B 12, epr spectroscopy, 433-442 23-106 isomeric forms, nmr spectroscopy, 484 Cobalt: 13C-Iabelled, 474 alkylation, nitromethane, 280 nmr spectroscopy: cobalt complexes, electronegativity, fluxionality, 490 490 pH dependence, 493 coordination, 47 temperature dependence, 463-500 hydrides: nmr spectrum, 474 pK values, 335 nomenclature, 17 stability, 335, 365 nucleotide loop biosynthesis, 148 incorporation into: prototrophs, 155 15-cyano-l,2,2,7,7,12,12-heptamethyl- reaction with metal ions, 495 corrin, 211 secondary alkyl, 255 vitamin B 12, 211 zinc, 253 model systems, 378 Cobalocorrin, structure, 203 organic radical rearrangements, role of, Cobaloxime, structure, 246 533

Cobaloxime-BF2 bridged, nucleophilicity recombination with alkyl radicals, 335 cobalt(I), 251 reduced, X-ray crystallography, 69 Cobaloxime, structure, 246 reduction by alkali, B128 formation, 226 Cobaloximes: role in vitamin B12 chemistry, 333, 335 addition to olefins, mechanism, 264 unique biologically, redox chemistry, 340 alkylation: Cobalt 15-cyano-2,2,7,7,12,12-hexamethyl- hydrazines and oxygen, 275 corrin: kinetics, table, 259 electronic spectrum, 424 aryl derivatives, 270 structure, 423 axial phosphines, bond lengths, 83 Cobalt 15-cyano-7,7,12,12,19-pentamethyl- bridged dimers, 268 corrin: chromatography, 247 electronic spectrum, 424 m-effect, 85 magnetic circular dichroism, 424 cobalt ligand bond distances, tables, Cobalt 15-cy ano-7,7,12,12-tetramethyl- 82-84 corrin: dimethylsulfide complexes, 248 electronic spectrum, 424 electronic spectrum, charge-transfer, structure, 423 419 Cobalt 2,2,7,7,12,12,15-heptamethylcorrin folding, 59 electronic spectrum, 424 structure, 423 hydrogen reduction, 252 Cobalt 2,2,7,7,12,12-hexamethylcorrin: intramolecularly bridged, 269 electronic spectrum, 424 MO-calculations, 419 structure, 423 model for corrin, 419

Cobalt 7,7,12,12-tetramethylcorrin: model systems, vitamin B 12 coenzyme, electronic spectrum, 424 551 structure, 423 modified cobalamins, 65 Cobalt carbenes, 576 nucleophilic attack, 527 Cobalt-carbon bond: radical transfer, 526 activation enthalpy: thalium(III),526

homolytic cleavage, 511 vitamin B 12 coenzyme, acid 312, enzymic kinetics, 511 reactions, 507, 547 biosyn hesis: covalent, comparison to C-C bond, 337 eukaryotes, 155 covalent bond, 335 prokaryotes, 155 dissociation energy determination: timing, 155 equilibrium, 507 bond angles: kinetics, 511 b-elimination, 369 photochemical, 507 protein effects, 373 thermochemical, 507 steric effects, 355, 372 distortion,protein, 373 bond dissociation energy: energies, 554 axial ligands, 531 energy, 1,4,8,11 -tetraazacy clotetra- conforma ional changes, 531 decanecobalt(III), 554 1-cyanoethylcobaloxime, 511 factors affecting bond dissociation energy,

isopropylcobaloxime, 511 VitaminB12 coenzyme, 531 1-methyl-heptylcobaloxime, 507, 511 formation: l-methyl-2-phenylethylcobaloxime, 511 alkylation, cobalt(III) complexes, 517 steric effects, 531 CoOEP, 279 bond lengths: halogen cleavage, stereochemistry, 317 isopropyl(pyridine)cobaloxime, 505 heterolytic cleavage, 305-319 isopropyl(tricyclohexylphosphine)- homolysis, enzymic reaction, 456 cobaloxime, 506 homolytic cleavage, 296, 362 isopropyl(triphenylphosphine)- I nsertion of dioxgen, 512 cobaloxime, 505 l abilization, protein, 333 methyl(aquo)cobaloxime, 505 labilization by steric interactions, 361 methyl(pyridine)£/s(acetylacetone)- l ength, alkylcobalt complexes, table, ethylenediiminecobalt, 505 505 methyl(pyridine)cobaloxime, 505 lengths, 54 methyl(triphenylphosphine)cobaloxime, alkylcobaloximes, 359 505 I sopropylcobaloxime, 359 vinyl(pyridine)Z>/s(salicylaldehyde)- metalloporphyrins, 246 ethylenediiminecobalt, 505 models for cleavage, vitamin B12 coenzyme, vinyl(pyridine)cobaloxime, 505 551 vitamin B coenzyme, 505 12 photochemical cleavage, 362, 524 bond strength, vitamin B coenzyme, 12 photolysis, 296 513 polarizability, nmr spectroscopy, 489 charge-transfer, electronic spectrum, 404 preparation, cobalt(III) complexes, cleavage: 271-277 corrin ring, distortion, 65 protection by peripheral groups, 90 cyanide, 306 protection by side chains, vitamin B 12 electrophilic, 526 coenzyme, 41 energetics, 551 pyrolysis, 303 halogens, 516, 526 reaction with electrophiles, 312-317 homolytic, 524 reductive cleavage: induction, vitamin B12 coenzyme, 550 carbon monoxide, 515 mercury(II), 526 thiols, 317,515 models, 88 role of 4s and 4p orbitals, 338

Cobalt-carbon bond (Cont'd) sodium reduction, 254 stability, 330, 335 trans-effect, nmr spectroscopy, 488 stability vs. metal, 339 see also Alkylcobalt complexes steric compression, distortion, 359 Cobalt corrin: steric crowding, bond length, 505, 506 bond angles, tables, 45-53 steric effects, bond dissociation energy, bond distances, tables, 45-53 512 folding, 60 synthesis: planarity deviations, 61 analysis of reaction mixtures, 247 torsion around A-D junction, 57 work up of reaction mixtures, 248 Cobalt-free corrin: thermal cleavage, 362 circular dichroism, 421 thermal dissociation, 1-phenylethyl- electronic spectrum, pH, 401 (pyridine)cobaloxime, 509 fluorescence spectrum, 402, 422 thermodynamic stability, 336 from Bacterium chromatium, 401 thermolysis: magnetic circular dichroism, 423 alkylcobalamins, 525 Cobalt-free corrinoid: alkylcobalt complexes, 525 electronic spectrum, 413

VitaminB12 coenzyme: luminescence, 426 acid decomposition, 366 Cobalt orbitals, interaction with corrin alkaline decomposition, 366 7r-orbitals, 561 cleavage, 547-554 Cobalt porphyrins, alkylation, diazo- 5 '-deadenosyl carbanion, and elimina- alkanes, 281

tion, 549 Cobalt role, vitamin B 12 coenzyme enzymic 5 '-deadenosyl carbocation, 548 reaction, 555 5 '-deadenosyl radical, 548 Cobalt(I) complexes: heterolytic cleavage, 548 acetylene, addition to, 256 homolytic cleavage, 548 acrylonitrile: stability, 366 addition to, 256 vitamin B 12s, photolysis, 297 olefin IT -complexes, 527

Cobalt-carbon intermediates, vitamin B12 addition to: coenzyme, 382 olefins, mechanism, 265 Cobalt complexes: unsaturated electrophiles, 256 alkylating agents, 254 a lkylation: alkylation, hydrazines and oxygen, 275 alkyl halides, 523 catalysis, sodium borohydride, 252 electron transfer, 259 cis-effect, nmr spectroscopy, 487 kinetics, 258 electronegativity, cobalt, 490 olefin addition, 523 hydrogen, reduction, 252 tereochemistry, 502, 523 mechanism, reductive alkylation, 258-267 alkylcobalt(III) complexes, trans- potassium, reduction, 254 alkylation, 527 redox chemistry, Schiff-base complexes, alkynes, addition to, 256

514 Cobaloxime-BF2 bridged, nucleophilicity, reduction: 251 chromium(II), 254 cobaloximes, nucleophilicity, 251 electrochemistry, 254 bis(l,2-cyclopentanedioximato) cobalt, sodium borohydride, 251 nucleophilicity, 251 thiols, 254 decomposition, 252 reductive alkylation, 250 diacetylmonoximeimino diacetylmono- reductive arylation, electron transfer ximatoiminopropane-1,3-cobalt, mechanism, 271 nucleophilicity, 251 rhodium corrin, comparison to, 72 threo-3,3-dimethylbuty 1-1,2,2- sodium amalgam reduction, 254 trifluoromethyl sulfonate, sodium borohydride reduction, 251 reaction wi h, 260

Cobalt(I) complexes (Cont'd) reactivity toward alkyl halides, table, effect of axial ligands, nucleophilicity, 521 252 spin-Hamiltonian, 436 electron-donor strength, ligand redox Cobalt(III) complexes: potential, 504 acetylene, carbanion reaction, 279 electronic spectrum, 262 alkylation: epoxides, reaction with, 256 acetone, 517 equilibrium, hydridocobalt complexes, diazoalkanes, 281 506 Grignard reagent, 277, 517 etheneimine, reaction with, 257 organolithium reagents, 517 mechanism, olefin addition, 262 carbenes, reaction with, 279 methylacrylate addition, 256 carbon monoxide, oxidation, 515 nmr spectroscopy, 486 cobalt-carbon bond: nucleophilicity: formation, alkylation, 517-524 effect of axial ligands, 252 preparation, 271-277 table, 251 electronic spectrum, 394 olefins, addi ion, 256 enols, reaction with, 279 phenylacetylene, addition, 256 ethyl vinyl ether, reaction with, 281 pH function, olefins, 523 2-hydroxyethylvinyl ether, reaction with, preferred coordination number, 504 282 propargyl alcohol, addition, 256 malononitrile, reaction with, 279 propyne addition, 256 nucleophilic attack, 284 reactions, 263 olefin 7r-complexes, 282 redox potential, table, 251 photoaquation, 296 stereochemistry, vinyl halides, photoreduction, 296 alkylation, 260 preferred, coordination number, 504 3,3,3-trifluoropropyne, addition, 257 reaction with: see also Cob(I)inamide; Hydridocobala- carbanions, 279 min; Hydridocobaloxime; Vitamin vinyl e hers, 281 12S stable, five coordinate, 506 Cobalt(II) complexes: zwitterionic, 286 alkylation: Cobalt(IY) complexes, 514 alkyl halides, 518 Cobalt(II) substrate radical separation, alkyl iodides vs. other alkyl halides, vitamin B 12 coenzyme enzymic 522 reaction, 452 radical intermediates, 518 Cobamic acid, nomenclature, 17 electronic structure, 438 Cobester, see Heptamethylcobyrinic acid epr spectroscopy, 433 Cobinamide guanosine diphosphate, halogen abstraction, alkyl halides, 274, 5,6-dimethylbenzimidazole-5 - 519 nucleotide, reaction with, 153 methyl radicals, recombination with, Cobinamide phosphate, addition of guano- 335 sine diphosphate, 152 nmr spectroscopy, 486 Cobinamides: orbitals, 438, 440 biosynthesis, 151, 152 organic radical interaction, epr spectrum, chemical synthesis, 152 450 circular dichrosim, 421 outer-sphere electron transfer, Schiff-base vs. cobalamins, alkylcorrins, 369 complexes, 519 electronic spectrum, 415 preferred coordination number, 504 enzymic preparation, 152 reaction with: epr spectroscopy, 442-448 alkyl halides, 273 equilibria, 5- and 6-coordinate, table, kinetics, 273, 274, table 350 organic radicals, 271 formation, 234

Cobinamides (Cont'd) Co [(CO)(DOH)pn], see Diacetylmono ximeimino a, b -isomers, electronic spectrum, 413 diacetylmonoximato- table, 416 iminopropane-l,3-cobalt; Cobalt steric interactions, epr spectrum, 448 complexes structure, 235 Coenzyme, see Vitamin B 12 coenzyme

from vitamin B 12, cerium(III) hydroxide, Coenzyme B 12 , see Vitamin B12 coenzyme 236 Coenzyme func ion, vitamin B12 s, 147

vitamin B 12 , conversion to, 234 Cofa ctor: Cobinic acid, nomenclature, 17 2,6-diaminohexanoate mutase, pyridoxal Cobyric acid: phosphate, 574 bond angles, tables, 45-53 glutathione, nucleotide loop biosynthesis. bond distances, tables, 45-53 152 cell dimensions, 94 Color and clinical activity, vitamin B12, 8 chemical formula, 94 Comparison to: circular dichroism, 421 cobalt complexes, rhodium corrin, 72 cobyric acid a and b , 197 crystal structure, conformations, 482 conversion to cobalamins, 148 model systems:

VitaminB12, 197 vitamin B 12 ,504 electronic spectrum, 415 vitamin B 12 coenzyme, 504 folding, 60 vitamin B 12 , nonvitamin B 12, 35 formation, 235 vitamin B 12 coenzyme, table, vitamin planarity deviations, 61 B12, 53 space group, 94 X-ray structure, nmr spectroscopy, molecular structure, 34, 148, 170 structure in solution, 482 torsion around A-D junc ion, Configurational interactions, electronic 57 spectrum, 398, 404 total synthesis, 187, 196 Configurations: trimethylated isobacteriochlorins, corrin, 209 incorporation into, 132 N-glycosides, cobalamins, 153

vitamin B 12 , conversion to, 235 Conformational changes: X-ray crystallographic data, 94 cobalt-carbon bond, bond dissociation X-ray diffraction data, diagram, 34 energy, 531

Cobyric acid a and b, 197 vitamin B 12 coenzyme, 374 Cobyrinic acid, acid hydrolysis, vitamin Conformations:

B 12, 230 alkylcobalamins, 341 biosynthesis: comparison to crystal structure, 482 origin of carbon atoms, 112 corrin, table, 50, 51 primary precursors, 111 corrin ring side chain, 52, 54, 63 uroporphyrinogen(III) as precursor, corrin side chain, 207, 341 116 electronic structure and spectrum, 343

Factor I: neovitamin B12, 209 incorporation into, 131 nickel( II) 15 -cy ano-7,7,12,12,19- reduced form, incorporation into, 131 pentamethylcorrin chloride, 208 nomenclature, 17 nucleosides, 70 sirohydrochlorin, incorporation into, nucleotide loop, 65 123 nucleotides, 70 structure, 109 side chain, 52, 54 uroporphyrinogen III, biosynthetic vitamin B 12 : precursor, 116 ribose ring, 550, 554 Cobyrinic acid a,c-diamide: side chain, 208 preparation, 37 Conjugated system: X-ray crystal structure (diagram), 34 addition to corrin, 238

Conjugated system (Cont'd) Copper analog, vitamin B 12 , 211 corrin, 61, 203 Copper cobalamin, magnetic circular dich- vitamin B 12, 238 roism, 426

Constraint of axial ligands, vitamin B12 Copper incorporation into vitamin B12, conezyme, 41 211 Conversion to: Correlation between nmr and electronic 2-alkoxyalkylcobaloximes, 2-acetoxy- spectrum, cobalamins, 418 alkylcobaloximes, 575 Corrin biosynthesis: D-l-amino-2-propanol, L- hreonine, 199 bilanes: 15-carboxy-l5-norcobinamide, vitamin aminomethyl, 117

B 12, 239 hydroxy methyl, 118 cobalamins, cobyric acid, 148 1-methyl, 121

cobinamides, vitamin B12 , 234 broken cell enzymes, 116

cobyric acid, vitamin B 12 , 235 cell free enzymes, 116 dicyanocobalamin, standard electronic decarboxylation, C-12, first step, 120

spectrum for vitamin B 12 , 395 porphobilinogen deaminase, 117 heptamethyl dicyano-5, 15-bisnorcobyri- secocorrins, intermediates in, 116

nate, vitamin B12, 239 spirocyclic intermediate, 118 heptamethyl dicyanocobyrinate, vitamin uroporphyrinogen III, loss of, C-20, 137,

B 12, 236 139, 145-167 c/s-isoketipinic acid, (+)camphor, 174 Corrin p-orbitals, cobalt orbitals, interactions, 561

methylcobalamin, vitamin B 12 coenzyme, Corrin precursor, aminomethylbilane, 163 117 sirolactone, sirohydrochlorin, 123 Corrin reduction, ferredoxin, 254

vitamin B12, cobyric acid, 197 Corrin ring:

vitamin B12 coenzyme, cobalamins, 156 S-adenosylmethionine, activation, 345 methylcobalamin, 163 C-10 chemical shifts vs. electronic CoOEP, cobalt-carbon bond formation, 279 spectrum, 487 5- and 6-Coordinate: conjugation, 61 alkylcobalamins, 346, 351 deforma ions, 63 cobinamides, equilibria, 350 5 '-deoxyadenosyl ligand, interactions corrin, axial ligands, 346 with, 66 homolytic cleavage, 371 5,6-dimethylbenzimidazole, interaction

vitamin B 12 coenzyme, 346 with, 28,353 Coordination: distortion, cobalt-carbon bond cleavage, alkylcobalamins, cw-diaminoplatinum(II), 65 495 folding, benzimidazole effect on, 59, alkylcorrins, imidazole, 358 60 (table) cobalamins, cw-diaminoplatinum(II), 495 gadolinium(III), shift reagent, 472, cobalt, 47 482 mercury(II), cobalamins, 495 nmr spectrum: l-(2-trifluoromethylphenyl)imidazole, C-10 proton, 469 heptamethylcobyrinate, 495 lanthanide shift reagents, 471, 482

vitamin B 12 coenzyme, c/s-diamino- paramagnetic shifts, 471 platinum(II), 497 1H/2 H exchange, 469 13 vitamin B 128, 5,6-dimethylbenzimidazole, nmr spectrum( C), 479 486 side chain, 480 Coordination chemistry: planarity, 54 adenylcobamide, 351 puckering, 54

vitamin B 12, 325-392 side chain, conformations, 52, 54, 63

Coordination number, cobalt complexes, vitamin B 12 coenzyme, nmr spectrum, 504 469

Corrin: dimethyl(methylene)ammonium iodide, adenosylation, 155 reaction with, 213 affinity chromatography, 268 distortion, 207 alkylation, 214 electronic spectrum, polarization effects, alkyl ligands, effect on physical properties, 393-430 table, 356 electrophilic substitution, MO-calcula ions, 5-aminolevulinic acid, incorporation into, 212,345 111 electrophoresis, 249 aromaticity, 204 epimerization, equilibrium constants, axial ligands: table, 222 5- and 6-coordinate, 346 mechanism, 224 steric requirements, 255 MO-calculations, 220 bioxynthesis: trifluoroacetic acid, 222 Euglena gracilis, 117 epimers, 210 1-methylbilane, 107-144 folding, 60 Propionibacterium shermanii , 112 halogenation, 204, 215 bond angles, di stances, table s, 45-53 helicity, 209 bond lengths, observed and calculated, hydrated electrons, reaction with, 318 205,48 table, 49, 206 Ion exchange chromatography, 249 bromination, 215 13C-Iabelled, 474 buckling, 208, 342 lack of aromaticity, 204 canonical resonance structures, 205 lactam formation, 225 charge-transfer, 403 lactone formation, 226 chirality, 209 laser Raman spectrum, 343 chiroptic effects, 207 ligand substitution roles, 330 chloramine T, reac ion with, 215 ligand substitutions, 337 chlorosulfonyl isocyanate, cyanation, luminescence, 426 213 cobalt-free, 426 chromatography: macrocycle reactions, 201-243 carboxymethylcellulose, 249 magic Mannich, dimethylaminome hyla tion, DEAE cellulose, 249 213 phosphocellulose, 249 magnetic properties, 330 separation of neo and normal, 222 meso-methyl groups: Sephadex, 247, 249 oxidation, 239 circular dichroism,a, 0-isomers, 420-426 pKa values, 239 cis-effect, nmr spectroscopy, 330, 487 meso-substitution, 212 Clostridium tetanomorphum, source of, metal-free, electronic spectrum, 207 146 metallation, 210-212 configurations, 209 methionine: conformations, 50, 51, 207, 341 incorporation into, 111

conjugated system, addition to, 203, 238 CD3 -methyl, incorporation into, 114 5-coordinate, decomposition, alkyl p -molecular orbitals, 397 cobalamins, 369 nitrosation, 217 crystallization, 249 nitrosyl chloride, reaction with, 217 cyanation, 213 nmr spectroscopy, 463-500 cyclization (peripheral): nomenclature, 18 lactam formation, 225 nucleotide loop biosyn hesis, 148 lactone formation, 226 orbital energies, 206, 399 xanthocorrinoids, 228 organic solvent soluble, prepara ion, 236 dehydrogenation, 238 organocobalt complexes, (review), 330 demetallation, 210 oxidation: deuteration, 212, 220 carboxylic acids, 218 dimethylaminomethylation, 213 chromic acid, 218

Corrin (Cont'd) Coupling east and west halves, vitamin B 12 hydrogen peroxide, 218 total synthesis, 169-200 oxidative cleavage, succinimides, 217-220 Covalent bond, cobalt-carbon bond, 335 ozonolysis, secocorrindione, 218, 219 CrystalUzation: paper chromatography, 249 alkylcobaloximes, 248 permanganate oxidation, 218, 219 corrin, 249 pentadecaalky! from vitamin B 12, 236 Crystal morphology:

circular dichroism, 237 pleochroism vitamin B12 , 26

phenol extraction, 249 refractive index, vitamin B 12 , 26 phenylthiomethyl chloride, reaction with, Crystal structure, conformations, comparison 214 to, 482 photoaquation, 330 Cyanation: planarity, deviations, 61, 208 corrin, chlorosulfonyl isocyanate, 213

porphobilinogen, incorporation into, 111 vitamin B 12, 213 Propionibacterium shermanii, source of, Cyanatocobalamin, electronic spectrum, 146 411 radical recombination, 363 Cyanide: resonance Raman spectrum, 398 acetonitrile formation, methylcobaloxime, secocorrindione cyclization, 219 307 side chain conformations, 63, 208 L-adenosylcobalamin, reaction with, 306 sign inversion, circular dichroism, 422 ara-adenosylcobalamin, reaction with, 306 steric effects: alkylcobalamins, reaction with, 306 origin, 355 aristeromycyclocobalamin, reaction with, transmission, 355 306 strain orbital, 400, 411 N-benzoyladenosylcobalamin, reaction torsion around A-D junction, 57 with, 306 trans-effect, nmr spectroscopy, 80, 330, Coa-adenyl-Co/3-adenosylcobalamin, 487 reaction with, 305 uroporphyrinogen III, intact incorpora- Coa-aquo-Co/3-adenosylcobamide, reac- tion into, 117 tion with, 306 varia ion with temperature, electronic Coa-aquo-Co/3-adenosyl(3,5,6-trimethyl- spectrum, 348 benzimidazolecobamide), reaction see also Cobalamin; Metallocorrins; wi h, 306 Specific metallocorrins; Yellow corrinoids cobalt-carbon bond cleavage, 306 Corriphyrin-3: difluorochloromethylcobalamin, reaction isolation, 134 with, 307 nmr spectrum, 135 D-erythro-2,3-dihydroxy-4-pentenal, structure, 134 vitamin B 12 coenzyme, 305 Corriphyrin-4, structure, 124, 128 formycyclobalamin, reaction with, 307 Corriphyrins, 121. Seealso pyrazolopyrimidine nucleosidylcobalamin, Sirohydrochlorin reaction with, 307 Corrole: N-tosylcytidylcobalamin, reaction with, bond angles, distances, tables, 45-53 306 folding, 60 triethylaminoethylcobalamin, reaction nomenclature, 19 with, 307 structure, 203 trifluoromethylcobalamin, reaction torsion around A-D junction, 57 with, 307 Cosynthetase, see Uroporphyrinogen III vitamin B 12 coenzyme, reac ion with, 305 cosynthetase 15-Cyano-l,2,2,7,7,12,12-heptamethyl- CoTPP, disproportionation: corrin: alkylation, 279 bond lengths, 206 in basic DMSO, 279 cadmium, incorpora ion into, 211 cobalt incorporation into, 211

15-Cyano-l,2,2,7,7,12,12-heptamethyl- Cyclobutylcobalamin, rate of decom- corrin (Cont'd) position, 368 electronic spectrum, 401 Cyclodecyl-I-d-iodide, reaction with

lithium, incorporation into, 211 vitamin B128, 261 metallation, 211 Cyclohexylcobalamin: nickel, incorporation into, 211 electronic spectrum, 255 rhodium, incorporation into, 211 rate of decomposition, 368 structure, 211 CyclohexylcobaJoxime, thermolysis, zinc, incorporation into, 211 304

15-Cyano-l, 2,2,7,7,12,12-heptamethyl- Cyclohexylnitrone, vitamin B 12 total corrin hydrochloride: synthesis, 192 cell dimensions, 95 Cyclohexyl-3, 5, 6-trimethylbenzimidazoyl- chemical formula, 95 cobamide, preparation, 255 space group, 96 Cyclopentylcobalamin, ra te o f decomposi- X-ray crystallographic data, 96 tion, 368 Cyano-1,8,8,13,13-pentamethyl-5-cyano- Cyclopropane formation, pentacyanocobaltate 16-ethoxy-14-[2-imino-propenyl] - 1,3-diiodopropane, 519 CD secocorrin perchlorate: Cyclopropylcarbinylcobalamin r earrange- cell dimensions, 97 ments, but-3 -enylcobalamin, 362, chemical formula, 97 379,567 space group, 97 Cyclopropylcarbinylcobaloxime rearrange- X-ray diffraction data, 97 ments, 381 Cyanoaquocobinamide, a,b-isomers, nmr Cyclopropylcarbinyl(pyridine)cobaloxime spectrum, 484 rearrangements, but-3-enyl-

Cyanobromide vitamin B 12, total synthesis, (pyridine)cobaloxime, 568 169-200 Cyclopropylcarbinyl radical rearrange- Cyanocobalamin: ments, but-3-enyl radical kinetics,

vitamin B12, 17 557,567

see also Vitamin B12 Cyclopropylcobalamin, rate of decomposition,

R-a -cyanoethyl(S-a -methylbenzylamine)- 368 cobaloxime, racemization, X-ray Cyclopropyloxycorrinoid, 570 crystallography, 88 Cylindrical projection, X-ray structure, Cyanoethylcobalamin: 97 alkaline decomposition, 366 Cysteinylcobalamin, ele ctronic spectrum, reaction with alkali, 310 411 1-Cyanoethylcobaloxime, cobalt-carbon Dansylamidopropylcobalamin pr eparation, bond, bond dissociation energy, 267 511 DBC, see Vitamin B12 coenzyme Cyanoimidazolecobinamide, electronic DEAE cellulose, corrin chromatography, spectrum, 343 249 Cyanomethylcobaloxime, thermolysis, 304 Dealkylation alkylcobalamins, thiols, Cyclic nucleoside, structure, 554 alkylcobaloximes, 527 Cyclic 2', 3', -ribazole phosphate, Deamidation, nicotinate mononucleotides,

vitamin B 12 total synthesis, 153 194 Deaminase, see Porphobilinogen deaminase 8, 5'-Cyclic-adenosine, see 5'-Deoxy-8, 5'- Deamination: cycloadenosine aminomethylbilanes, porphobilinogen Cyclization: deaminase, 117 corrin, secocorrindione, 219 bilanes, aminomethyl, 118 5 '-deoxyadenosyl radical, 554 Decarboxylation: lactam formation, corrin, 225 C-12, first step in corrin biosynthesis, lactone formation, corrin, 226 120 xanthocorrinoids, corrin, 228

Decarboxylation (Cont'd) VitaminB12 coenzyme: 15-carboxy-15-norcobinamide, 239 ribonucleotide reductase, 577 5,15-dicarboxy-5,15-dinorcobinamide, thiols, photolysis, 299, 545 239 [5'-3H]5'-deoxyadenosine, 298 [R] -l-amino-2-propanol, threonine, 5 '-Deoxyadenosyl carbanion, 549 150 5'- Deoxyadenosyl carbocation, stabiliza tion, Decomposition: 549 in acid, j3-hydroxyethylaquocobaloxime, 5 '-Deoxyadenosyl ligand: 313 interactions with corrin ring, 66 13 acid catalysis, alkylcorrins, 369 nmr spectrum( C), 477 alkylcobalamins: 5 '-Deoxyadenosyl ligand, vitamin B12 corrin five coordinate, 369 coenzyme, nmr spectrum, 468 2 rate of, 365,368,370 5 - H -Deoxyadenosyl ligand, nmr spectrum, very strained, rate of, 371 VitaminB12 coenzyme, 471 alkylcorrins, olefins, 365 5'- Deoxyadenosyl radical: 1-chloro-2,2-Z>w(p-chlorophenyl)ethyl- cyclization, 554 cobalamin, trans-4, 4'-dichloro- formation: stilbene, 304 8-position modification, 298 cobalt(I) complexes, 252 reactions, 297, 363 cyclobutylcobalamin, rate, 368 reaction with vitamin B12r, 373 cyclohexylcobalamin, rate, 368 stabilization, 548 cyclopentylcobalamin, rate, 368 vitaminB12 coenzyme: cyclopropylcobalamin, rate, 368 enzymic reaction, 554 methylcobalamin, rate, 368 ribonucleotide reductase, 577 neopentylcobalamin, rate, 368 5 '-Deoxy-8,5 '-cycloadenosine: 2- norbornylcobalamin, rate, 368 formation, 297 structure, 297 Decyanation, vitamin B12 , ferredoxin, 6 163 5'-Deoxy(l,N -etheno)-adenosylcobalamin, Deficiency, cobalamins, 157 preparation, 285 Definition, nucleophilicity, 250 5 '-Deoxy-5 '-halonucleoside preparation, Deformations, corrin ring, 63 vitamin B 12 coenzyme analogs, 267 Dehalogenation, vitamin B 12 , 217 Dehydration: Dephosphorylation, cobalamin phosphate, 1,2-dihydroxyethyl radical, 573 154 yellow corrinoids, 229 D -erythro -2,3-Dihydroxy-4 -pentenal, Dehydrocobinamide: vitamin B 12 coenzyme and chromic acid oxida ion, 226 cyanide, 305 mechanism of formation, 226 Descobaltocobalamin, metallation, 211 Descobaltocobantide: see also Lactams (corrin ring) Dehydrocorrin: electronic spectrum, pH, 211 metallation, 211 bond angles, distances, tables, 45-53 Descobaltocobyric acid, 211 torsion around A-D junction, 57 Desulfoviridin, sirohydrochlorin isolation, Dehydrogenation, corrin, 238 122 Dehydrovitamin B 12 chlorination, 215 Deuteration: corrin, 212, 220 structure, 215 dicyanocobalt(III) tetramethylcorrin, Demetallation: 212 corrin, 210 ethylcobinamide, 345 siroheme, 128 metallocorrins, 220 vitamin B 12, 210 vitamin B , hexacarboxylic acid, 212 5 -Deoxyadenosine, 441, 558 12 see also 1 H/2 H exchange hydrogen abstrac ion, 554 Deviations from planarity, corrins, 61 intermediate, vitamin B 12 coenzyme, 332

Diacetylmonoximeimino diacetyl- trans-4,4'-Dichlorostilbene, decom- monoximatoiminopropane-1,3- position l-chloro-2,2- cobalt: bis (p - chlorophenyl)- alkyl complexes, redox chemistry, 514 ethylcobalamin, 304 nucleophilicity, cobalt(I), 251, 523 Dicobaloximes, preparation, pKa values, 504 268 redox potential, 504 Dicyanocobalamin: structure, 503 electronic spectrum, 413 13 Diacetylmonoximeimino diacetylmono- nmr spectrum, C, biosynthetic ximatoiminopropane-1,3-cobalt(I): studies, 112 13 alkyl complexes, photolysis, 524 nmr spectrum, CN enriched, nucleophilicity, 523 478

2,6-Diaminobularine, vitamin B 12 coenzyme standard electronic spectrum, fluorescent analogs, 300 vitamin B 12, 395 13 2,6-Diaminohexanoate mutase, pyridoxal table ( C), nmr spectrum, phosphate co factor, 574 476 (R)-2,6-Diaminohexanoate, 546 Dicyanocobalt(III) tetramethylcorrin, (S)-3,6-Diaminohexanoate, 546 deuteration, 212 3.5- Diaminohexanoic acid, 328 Dicyanocobinamide: 2.5- Diaminonebutavinylcobalamin, circular dichroism, 421, 424 preparation, 267 electronic spectrum, temperature (R)-2,5-Diaminopentanoate, |3-leucine, variation, 348, 395, 408, 424 13 540,546 table ( C), nmr spectrum, 476 cis-Diaminoplatinum(II), coordination: Dicyanofcobyrinic acid-0,c-diamide]: alkylcobalamins, 495 cell dimensions, 94 cobalamins, 495 chemical formula, 94

vitaminB12 coenzyme, 497 space group, 94 2,4-Diaminovaleric acid, 328 X-ray crystallographic data, 94 Diaquocobinamide, formate reduction, Dicyanocobyric acid, structure, 206 447 Dicyanocobyrinic acid, abcdeg hexamethyl Diazene cobalt complexes, 275 ester/-nitrile, 214 Diazoalkanes: Dicyano-5,6- dihy droxy- dehydro-cobyrinic cobalt(III) complexes, alkylation, acid pentamethylester-c,cMactone, 281 see Yellow corrinoids cobalt porphyrins, alkylation, 281 Dicy an o-5,6-dihy droxy-dehydro-cobyrinic preparation, vinylcobalt porphyrins, hexamethy lester-c -lactone, see 280 Yellow corroinoids Diazomethane: Dicyanoheptame hylcobyrinate, magnetic esterification, basic conditions, vitamin circular dichroism, 426 Dicyano-5-hydro-6-amino-dihy dr o-cobyrinic B 12 total synthesis, 193 preparation of halomethylcobalt acid pentamethylester-fl-amide-c- porphyrins, 280 lactam, see Yellow corrinoids Dibenzo-corromin, X-ray crystallographic Dicyan o-5 -hydro - 6- amino - dihy dro- data, 92 cobyrinic acid pentamethylester- OL- ab-Dibromoethyl acetate, vitamin B 12 amide-c-lactam, see Yellow coenzyme reaction with, 285 corrinoids 5,15 -Dicarboxy-5,15 -dinorcobinamide: 4', 5 -Didehydro-5 '-deoxyadenosine, decarboxylation, 239 441 preparation, 239 4', 5 '-Didehydro-5 '-deoxyaristeromycin: 5,6-Dichlorobenzimidazole, X-ray diffraction formation, 297 structure, 297, 308 data, vitamin B12, 27 Dichloromethylcobalamin, photolysis, Diels-Alder, Lewis-acid catalyzed, vitamin 303 B 12 total synthesis, 183

2,2-Diethoxyethylcobalamin, preparation, Dimethylated isobacteriochlorins, 281 structure, 123 Diethylaminoethyl cellulose, see DEAE Dimethyl(bromomethyl)malonate, reaction

cellulose, corrin chromatography with vitamin B 12 s , 564 8,12-Diethyl-2,3,7,13,17,18-hexamethyl- corrole: Dimethyl(methylene)ammonium iodide, cell dimensions, 96 reaction with corrin, 213 chemical formula, 96 5,6-Dimethylbenzimidazole:

hydrobromide, X-ray crystallographic coordination, vitamin B 128 , 486 data, 96 dissociation, 494 space group, 96 interaction with corrin ring, 353 X-ray crystallographic data, 96 nmr Spectrum(13C), 477 Difference electron density map, X-ray 5 '-nucleoside, 154 structure, 97 pK values, 351 Difluorochloromethylcobalamin, reaction protonation, nmr spectroscopy, 494 with cyanide, 307 steric interaction with corrin ring, epr Dihalomethylcobaloximes, reaction with spectrum, 448 alkali, 309 thermodynamics, Ugand exchange, table, Dihydromethylisobacteriochlorin, 141 496 Dihydrosirohydrochlorin, 139 trans-cfted, nmr spectroscopy, 488

Dihydroxyalkylcobaloximes, preparation, vitamin B 12 coenzyme, nmr spectrum, 284 465,470

Dihydroxyalkylcobalt complexes, models vitamin B 12 , total synthesis, 198 for enzymic reaction, 572 5,6-DimethylbenzimidazoIecob(II) inamide,

1,2-Dihydroxyalkyl radicals, vitamin B 12 epr spectrum, 448 coenzyme, diol dehydrase, 571 5,6-Dimethylbenzimidazole-5 '-nucleotide, 1,2-Dihydroxyethylcobalt, olefin 7r-com- reaction with cobinamide guanosine plexes, 574 diphosphate, 153

2,2-Dihydroxy ethyl cobalt, olefin p threo-3,3-Dimethylbutyl-l,2-tf 2 2-trifluoro- complexes, 574 methyl sulfonate, reaction with 1,2-Dihydroxyethyl radical: cobalt(I) complexes, 260 dehydration, 573 fra^s-Dimethylcobalt(III) complexes, pulse radiolysis, 574 heavy metal alkylation, 527 rearrangements, 532 Dimethylmercury(II), methylcobalamin, 4,5-Dihydroxy pentylcobaloxime: 526 1,2-dihydroxypentyl radical, 573 Dimethylsulfide complexes, cobaloximes, photolysis, pentanal, 534, 573 248 1.2- Dihydroxypentyl radical, 4,5-dihydroxy- Diol dehydrase:

pentylcobaloxime, 573 1,2-dihydroxyalkyl radicals, vitamin B 12 Dihydroxypropylcobalamin: coenzyme, 571 Dihydroxypropylcobalamin: enzymic reaction, bridged cation, 546, glyceraldehyde, photolysis, 302 555 glyceric acid, photolysis, 302 epr spectroscopy, enzymic reaction, 558 2.3- Dihydroxy-H-propylcobalamin: inhibition, nitrous oxide, 373 periodate oxidation, 284 MO-calculations, 557

photolysis, 302 model systems, vitamin B 12 coenzyme, 1,3-Diiodopropane, cyclopropane formation, 532,571 pentacyanocobaltate, 519 radical intermediates, 556 Dimeric complex with iodide, heptamethyl- reaction pathways, olefin ^-complexes, cob(II)yrinate, 522 555,558,575

Dimethylaminomethylation, corrin, magic vitamin B 12 coenzyme, enzymic reaction, Mannich, 213 529

vitamin B 12 , 213 1,2-Diols, radical rearrangements to alde- hydes, 573

1,3-Dioxa-2-cyclopcntylmethylcobaloxime, Electrochemical oxidation: preparation, 282 alkylcobaloximes, 515 1,3-Dioxo-2-cyclopentylmethylcobalamin, methylcobalamin, 517 reaction with acid, 315 see also Redox chemistry; Redox potentiall Dioxygen, cobalt-carbon bond insertion, Electrochemical reduction: 512 cobalt complexes, 254 Dipolar coupling, epr spectroscopy, 452 methylcobalamin, 318 Direct methods, X-ray structure, 97 methylcobinamide, 318 Disproportionation: Electrocyclic ring opening, enzymic

alkylation, CoTPP, 279 reaction, vitamin B 12 coenzyme, in basic DMSO, CoTPP, 279 576 cob(II)aloximes, 253 Electron d ensity map, X -ray str ucture,

vitamin B 12r ., 253 97

vitamin B 12s , vitamin B 121 ., 514 Electron ( hydrated), cobal amin r educ- Dissociation energy: tion, 254 equilibrium, cobalt-carbon bond, 507 Electron-donor strength, ligand redox kinetics, cobalt-carbon bond, 511 potential, cobalt(I) complexes, photochemical, cobalt-carbon bond, 504 507 Electronegativity, cobalt complexes, 490 thermochemical, cobalt-carbon bond, Electronic spectrum: 507 alkylcobaloximes, 406 Dissociation-recombination pathway, aminocobalamin, 411 aquocobalamin, 417 vitamin B 12 coenzyme, enzymic reaction, 555 aquocyanocobinamide, 408, 413 Distortion: aquohydroxocobinamide, 413 cobalt-carbon bond, steric compression, axial ligands, 409, 412 359,373 azidocobalamin, 411, 417 cobalt-carbon bond cleavage, corrin ring, calculations, vitamin B 12 coenzyme, 65 398 corrin, 207 carboxymethylcyanocobalamin, 413 charge-transfer, cobaloximes, 394, 403, vitamin B 12 coenzyme, protein role, 372 419 DMBC, see Vitamin B 12 coenzyme a-Donor power, ligands, 333 10-chlorodehydrovitamin B 12 , 215 cob(I)inamide, 419

E. coli: cob(II)inamide, 418 alkaline phosphatase, cobalamin phosphate cobalamins: dephosphorylation, 155 bound to human intrinsic factor, table, methylcobalamin, biosynthesis, 161 417 El/2, see Redox potential correlation between nmr and, 418 cobaloximes, 419 E2, see Vitamin B 12 , carboxylic acids, cobalt-carbon bond, charge-transfer, preparation; Vitamin B 12 , mono- carboxylic acid 404 Effect of axial ligands: cobalt 15 -cy ano-2,2,7,7,12,12-hexa- alkyl ligands, pK values, 356 methylcorrin, 424 alkyl ligands, table, electronic spectrum, cobalt 15 -cy ano-7,7,12,12,19-penta- 356 methylcorrin, 424 7-band, electronic spectrum, 411 cobalt 15 -cyano-7,7,12,12-tetramethy 1- cobalt(I) complexes, nucleophilicity, corrin, 424 250,252 cobalt 2,2,7,7,12,12,15-heptamethyl- Effect on corrin ring folding, benzimidazole, corrin, 424 59 cobalt 2,2,7,7,12,12-hexamethylcorrin, Effect on physical properties, corrin alkyl 424 ligands, 356

Electronic spectrum (Cont'd) 10-nitrosocobalamin, 217 cobalt 7,7,12,12-tetramethylcorrin, octamethyl ester, trimethylated 424 isobacteriochlorins, 132 cobalt(I) complexes, 262 pH: cobalt(III) complexes, 394 cobalt-free corrin, 401 cobalt-free corrinoid, 413 descobaltocobamide, 211 cobinamides, a, /3-isomers, 413, table, 415 phenolatocobalamin, 404 cobyric acid, 415 polarization effects, corrin, 402 configurational interactions, 398, 404 n -propylcyanocobalamin, 413 conformations, electronic structure, 343 pyridinatocobalamin, 411 corrin: selenocyanatocobalamin, 411 metal-free, 207 sirohydrochlorin, octamethyl ester, variation with temperature, 348, 393- 123 430 solvent effects, 409 corrin ring, C-IO chemical shifts, 487 spin-forbidden transi ions, 406 cyanatocobalamin, 411 sulfitocobalamin, 347, 411 cyanoimidazolecobinamide, 343 sulfomethylcyanocobalamin, 413 15 -cyano-1,2,2,7,7,12,12-heptame thy 1- temperature effects, 407 corrin, 401 temperature variation: cyclohexylcobalamin, 255 alkylcobinamides, 348 cysteinylcobalamin, 411 dicyanocobinamide, 348 dicyanocobalamin, 413 isopropylcobinamide, 348 dicyanocobinamide, 395, 408, 424 methylcobinamide, 348 effect, alkyl ligands table, 356 tetracarboxylic acid, 415 effect of axial ligands, table, 7-band, theoretical considerations, 396 411 thiocyanatocobalamin, 411 enzyme-substrate complex, 375 trifluoroethylcyanocobalamin, 413 ethylcobalamin, 408 vibrational components, 403 ethylcobinamide, 408 vinylcobalamin, 346, 350, 415 ethylcyanocobalamin, 413 vinylcobinamide, 408 ethynylcobalamin, 411, 415 vinylcyanocobalamin, 413

Factor I, 130 vitamin B 12: hydridocobalamin, 365 bound to intrinsic factor, 414 hydroxocobalamin, 404, 417 chlorination, 215 hydroxyethylcyanocobalamin, 413 hexacarboxylic acid, 417 imidazolecobalamin, 411 lactam, 417 iodocobalamin, 411 lactone, 417 isopropylcobalamin, 255, 408 pentacarboxylic acid, 417 isopropylcobinamide, 255, 408 solvent effects, 207, table, 343, LCAO-MO, 396 393-430

metal-free corrin, 395 vitamin B 12 coenzyme: metallocorrins, 424 base-on, off, 357 me hylcobalamin, 408, 415 flash photolysis, 299 me hylcobinamide, 343, 408 photolysis, 296 methylcyanocobalamin, 413 solvent effects, 343, table, 350, 408, me hylisocyanatocobalamin, 411 410

modification of corrin ring, 415 vitamin B 12r , 41 8

neocorrinoids, 222 vitamin B 12s, 418 nephelauxetic series, 409 zinc 15 -cyano-2,2,7,7,12,12-hexamethyl- nickel 15-cyano-7,7,12,12,19-pentamethyl- corrin, 424 corrin, 424 Electronic structure: nickel 7,7,12,12,19-pentamethylcorrin, cobalt(II) complexes, 438 424 corrinoids, nmr spectroscopy, 487

Electronic structure (Cont'd) s-bonded organocorrinoids, vitamin B 12 electronic spectrum, conformations, 343 coenzyme, 547 Electron transfer: bridged cation, diol dehydrase, 555 bis(salicylaldehyde)e hylenediimine- cobalt-carbon bond cleavage: cobalt(II)(methylimidazole), homolysis, 456

halogen abstraction, 519 vitaminB 12 coenzyme, 507, 547

cobalt(I) complexes, alkylation, 259 cobalt role, vitamin B 12 coenzyme, 555 mechanism, cobalt complexes reductive cobalt(II) substrate radical separation,

arylation, 270 vitamin B 12 coenzyme, 452

vitamin B 12 coenzyme, enzymic reactions, 5 '-deoxyadenosyl radical, vitamin B12 547 coenzyme, 554 migration of group X, 555 dihydroxyalkylcobalt complexes, models Electrophiles, cobalt-carbon bond, reaction for, 572 with, 312-317 diol dehydrase: Electrophilic attack, MO-calculations, epr spectroscopy, 558

vitamin B 12, 212 vitaminB12 coenzyme, 529, 546 Electrophihc cobalt-carbon bond cleavage, dissociation-recombination pa hway,

526 vitamin B 12 coenzyme, 555 Electrophilic decomposition, alkyl- electron transfer, vitamin B12 coenzyme, cobalamins acid catalyzed, 527 547 Electrophilic substitution: corrin, 345 epr spectroscopy: MO-calculations, corrin, 212 organic radicals, 559 Electrophoresis, corrin, 249 radical doublet intermediates, 450 b-Elimination: VitaminB12 coenzyme, 431-462, 558 alkylcobaloximes, 364 ethanolamine ammonia-lyase: cobalt-carbon bond, 362 epr spectroscopy, 558 cobalt-carbon bond angles, 369 vitamin B 12 coenzyme, 529 reversibility, 367 vitamin B 12r -substrate radical separa- thermolysis, cobalt-carbon bond, 304 tion, mechanism, 453, 546

vitamin B 125 , isopropylcobalamin, 364 glutamate mutase, vitamin B12 coenzyme,

ENDOR, vitamin B 12r , 441, 442 529 Energerics, cobalt-carbon bond cleavage, glycerol dehydrase, 546 2 551 H intermediates, epr spectrum, vitamin Energies, cobalt-carbon bond, 554 B 12 coenzyme, 450 Enhancers, epr spectroscopy, 447 hydrogen abstraction, vitamin B12 Enols, reaction with cobalt(III) complexes, coenzyme, 554 279 hydrogen exchange, vitamin B12 coenzyme,

Enzyme bound vitamin B12 coenzyme, 554 449 Enzymes: hypothetical pathways, vitamin B12 corrin biosyn hesis: coenzyme, 547 broken cell, 116 kinetic isotope effect, vitamin B 12 cell free, 116 coenzyme, 554 Enzymic formation: methylcobalamin, 528

vitamin B 12r , 157 methylmalonyl-CoA mutase, 546

vitamin B 12s , 158 vitamin B 12 coenzyme, 529 Enzymic prepara ion, cobinamides, 152 MO-calculations, vitamin B 12 coenzyme, Enzymic reaction: 557

active site thiol, vitamin B12 coenzyme, model systems, vitamin B12 coenzyme, 555 501-541,564-577 aminomutases, 546 organic radicals, vitamin B12 coenzyme, 2-amino-l-propanol, radical inter- 547 mediates, 450 oxidative addition, vitamin B12 coenzyme, 576

Enzymic reaction (Cont'd) Epr signals during catalysis, vitamin B12 protein role, vitamin B 12 coenzyme, 555 coenzyme, 332 radical doublet intermediates, vitamin B12 Epr spectroscopy: coenzyme, 450 alkylcobaloximes, photolysis, 524

rapid reaction intermediate, vitamin B12 angular anomalies, cob(II)inamides, coenzyme, 455 443

reaction pathways, vitamin B 12 coenzyme, anisotropic hyperfine interaction, 555 cob(II)inamides, 443

reversibility, vitamin B 12 coenzyme, 545 carbon-skeleton, 381 ribonucleotide reductase: cob(II)amides, fifth axial ligands, 444 epr spectroscopy, 558 cobalamins, 433-442 epr spectrum, 451 cobalt(II) complexes, 433

VitaminB12 coenzyme, 529 cobinamides, 442448

table, vitamin B12 coenzyme, 546 dipolar coupling, 452

theoretical studies, vitamin B 12 coenzyme, enhancers, 447 557 enzymic reaction:

vitamin B 12r as intermediate, vitamin B12 diol dehydrase, 558 coenzyme, 530 ethanolamine ammonia-lyase, 558

vitamin B 12r: ribonucleotide reductase, 431-462, intermediate, 381 558 organic radical interaction, epr spectrum, function of fifth ligand, table, cob(II)- 450 inamides, 444 Enzymic reduction, aquocobalamin, 157 hyperfine splitting, 436 Enzymic role, olefin p-complexes, vitamin isomerase reac ions, 381

B 12 coenzyme, 534 isotropic exchange, 452

Epicobalamin, see NeovitaminB 12 monoclinic model, vitamin B 12r, 440 8-Epicobalamin, structure, 225 organic radicals, enzymic reaction, 13-Epicobalamin, structure, 224 559 3-Epicorrinoids, 224. See also Neocorrinoids powder samples, vitamin B121., 439, 8-Epicorrinoids, 224 442 biological activity, neocorrinoids, 225 principal axes, vitamin B 12,., 440 circular dichroism, neocorrinoids, 225 radical doublet intermediates, enzymic see also Neocorrinoids reaction, 450 13-Epicorrinoids, 224. Seealso rapid reaction intermediate, epr Neocorrinoids spectrum, 455 Epimerization: single crystals, vitamin B 121 ., 442 equilibrium constants, corrin, table, 222 theory, 435 mechanism, corrin, 224 vitamin B 12 coenzyme, enzymic reaction, MO calculations, corrin, 220 449-458, 558 neocorrinoids, trifluoroacetic acid, 220, Epr spectrum: 222 alkylcobaloximes, cation radicals, 517 trifluoroacetic acid, corrin, 222 aquocob(II)inamide, 448 cob(II)inamides, oxygenation, 434, 458 Epimers: cobalt(II) complexes, organic radical corrin, 210 interaction, 450 VitaminB12, 210 cobinamides, steric interactions, 448 3-Episirohydrochlorin: 5,6-dimethylbenzimidazole, steric absolute configuration, 130 interaction with corrin ring, identity with Factor IIa, 129 448 structure, 129 5,6-dimethylbenzimidazolecob(II)inamide, Episulfides, vitamin B 12 total synthesis, 185 448 Epoxides, reaction with cobalt(I) complexes, enzymic reaction: 256 ribonucleotide reductase, 451

Epr spectrum (Cont'd) epr spectrum, 450 vitamin B 12r, organic radical inter action, inhibition, nitrous oxide, 373 450 MO-calculations, 557

epr spectroscopy, rapid reaction inter mediate, model systems, vitamin B 12 coenzyme, 455 571

high pH, table, cob(II)inamides, 447 olefin p-complexes, vitamin B12 coenzyme, nitroalkylcorrins, photolysis, 405 575

oxygenated vitamin B nr, 458 radical cations, vitamin B12 coenzyme, ribonucleotide reductase, rapid reaction 573 intermediate, 455 radical intermediates, 556 simulation: rapid reaction intermediate, 455

azidocob(II)inamide, 445 reaction pathways, vitamin B 12 coenzyme, histidine cob(II)amide, 445 555,573

simulation, cob(II)amides, table, 446 vitamin B 12 coenzyme, enzymic reaction,

vitamin B 12 coenzyme, enzymic reaction: 529 13 C intermediates, 450 vitamin B 12r -substrate radical separation: 2 H intermediates, 450 mechanism, enzymic reaction, 455

vitamin B 12r: table, 454 6 base-on, off, 299 1,N -Ethenadenosine, vitamin B 12 coenzyme oxygenation, 458 fluorescent analogs, 300 steric interactions, 434, 439, 442, 448 E heneimine, reaction with cobalt(I) Equilibria: complexes, 257 6 axial ligands, 345 1 ,N -Ethenoadenosylcobalamin, preparation, cobalt-carbon bond, dissociation energy 267 determination, 507 Ethoxycarbonylcobalamin, al kaline de- 5- and 6-coordinate, table, cobinamides, composition, 360 350 2-Ethoxyethylamine, vitamin B12 coenzyme Equilibrium constants: photolysis, acetaldehyde, 298 aquocobalamin, ligand substitution, b-Ethoxyethyl(pyridine) cobal oxime, 337 ethylene, a cid decompo sition, corrin, epimerization, 220 313 hydridocobalt complexes, cobalt(I) Ethylcobalamin: complexes, 506 electronic spectrum, 408 Equilibrium data, cob(II)aloximes, 504 nmr spectrum, 468, 474 Equilibrium determination, 1-phenylethyl- photolysis, 302 (pyridine)cobaloxime, bond solution thermolysis, 304 dissociation energy, 508 spin-lattice relaxation times, 492 Esr, see Epr spectroscopy; Epr spectrum; Ethylcobinamide: Epr signals during catalysis, vitamin deuteration, 345 electronic spectrum, 408 B 12 coenzyme Ester ammonolysis, vitamin Bl2 total Ethylcyanocobalamin, electronic spectrum, synthesis, 192 413 Ethylene: Esterification, basic conditions, vitamin B12 total synthesis, diazomethane, acid decomposition: b 193 -ethoxyethyl(pyridine) cobaloxime, Ethane, methylcobalamin photolysis, 300 313 Ethane-l,2-diol, see Ethylene glycol methoxyethylcobalamin, 313 hydroxyethylcobalamin, acid decomposi tion, Ethanolamine, vitamin B 12 coenzyme 313 photolysis, acetaldehyde, 298, Ethylene glycol: 328 acetaldehyde, methyl(aquo)cobaloxime Ethanolamine ammonia-lyase: photolysis, 571 enzymic reaction, 546 pulse radiolysis, acetaldehyde, 574 epr spectroscopy, enzymic reaction, 558

Ethylene glycol (Cont'd) electronic spectrum, vitamin B12 co-

vitamin B 12 coenzyme, photolysis, enzyme, 299 acetaldehyde, 298, 328 methylcobalamin, 300, 335, 363, 525, Ethyl vinyl ether, reaction with cobalt(III) 553 complexes, 281 methylcobaloxime, 405 Ethynylcobalamin, electronic spectrum, methylcobalt complexes, 525

411,415 vitamin B 12 coenzyme, 376 Euglena gracilis, corrin, biosynthesis, Fluorescence spectrum: 117 cobalt-free corrin, 402, 422

Eukaryotes: vitamin B 12,426 cobalt-carbon bond, biosynthesis, 155-163 Fluorescent analogs:

vitamin B 12 coenzyme, biosynthesis, 2,6-diaminobulorine, vitamin B 12 156-161 coenzyme, 300 1 2 H/ H exchange: formycin, vitamin B12 coenzyme, 300 6 corrin ring, nmr spectrum, 469 1,N -ethenadenosine, vitamin B12

nmr spectrum, vitamin B12 coenzyme, coenzyme, 300

468,469 vitamin B 12 coenzyme, 267, 285 Extraction, corrins by phenol, 249 Fluxionality, cobalamins, nmr spectroscopy, 490 Factor A: FMN, cobalamin reduc ion, 157

nomenclature, 17 FMNH 2 , methionine biosynthesis, 162 X-ray crystallographic data, 92 Folding, corrin derivatives, 59 Factor I: Formal oxidation state, alkylcobalt biosynthesis, 131 complexes, 514 electronic spectrum, 130 Formate reduction, diaquocobinamide, incorporation into cobyrinic acid, 131 447

isolation from C. tetanomorphum, 130 Formycin, vitamin B 12 coenzyme isolation from P. shermanii, 130 fluorescent analogs, 300 reduced form incorporation into: Formycinylcobalamin, preparation, cobyrinic acid, 131 267 tetrahydrochlorin, 131 Formycyclobalamin, reaction with cyanide, structure, 130, 131 307 Factor II, see Sirohydrochlorin Formylmethylcobalamin: Factor IIa: preparation, 283, 315 3-episirohydrochlorin, identity with, reaction with acid, 314 129 Formylmethylcobaloxime, preparation, see also 3-Episirohydrochlorin 315

Factor III: Frozen solution epr, vitamin B12 coenzyme 5-methoxybenzimidazole, 471 photolysis, 299 nmr spectrum, 471, 472 Factor Via, see Cobyric acid Gadolinium(III), shift reagent, corrin ring, FAD, cobalamin reduction, 157 472,482 Ferredoxin: GCoPSE: corrin reduc ion, 254 preparation, yellow corrinoids, 40

decyanation, vitamin B 12 , 163 structure, yellow corrinoids, 42 Fifth axial ligands, epr parameters, table, X-ray diffraction data, yellow corrinoids, cob(II)amides, 444 40

First crystallization, vitamin B 12 , 3 see also Yellow corrinoids Five coordinate: Glossary, X-ray crystallography, 97 cobalt(III) complexes, stable, 506 Glutamate mutase:

decomposition, alkyl cobalamins, 369 acrylate radical, vitamin B 12 coenzyme, Flash photolysis: 571 alkylcobalt complexes, 525 enzymic reaction, 546

Glutamate mutase (Cont'd) Halogenation:

glycinyl radical, vitamin B12 coenzyme, cis-effect, vitamin B12 , 216 571 corrin, 204, 215

model systems, vitamin B 12 coenzyme, lactam formation, 226

olefin p-complexes, vitamin B12 coenzyme, lactone formation, 226 571 me hylcobalamin, 216 radical intermediates, 556 sulfonatocobalamin, 216

reac ion pathways vitamin B 12 coenzyme, vitamin B 12, 226

571 VitaminB12 coenzyme, 216 vitamin B 12 coenzyme, enzymic reaction, Halogen cleavage: 529 alkylcobaloximes, 317 L-Glutamic acid, 328 benzylcobaloxime, 317 Glutathione, nucleotide loop biosynthesis, isopropylcobaloxime, 317 cofactor, 152 stereochemistry, cobalt-carbon bond, Glyceraldehyde, photolysis, dihydroxy- 317 propylcobalamin, 302 Halogens, cobalt-carbon bond cleavage, Glyceric acid, photolysis dihydroxypropyl- 516,526 cobalamin, 302 Halomethylcobaloximes, reaction with Glycerol dehydrase, enzymic reaction, 546 alkali, 308 Glycerol photolysis, dihydroxypropyl- Halomethylcobalt porphyrins, diazomethane, cobalamin, 302, 328 preparation, 280 Glycinyl radical, vitamin B 12 coenzyme, Heavy metal methylation, methylcobalamin, glutamate mutase, 571 528 N-Glycosides: Helicity: biosynthesis, enzyme isolation, 153 corrin, 209

cobalamins, configurations, 153 vitamin B12, 209 Glyglycobalamin, reac ion with, hydroxy- Heptamethylcob yrinate: lamine, 312 coordination, l-(2-trifluoromethylphenyl)- Gold(I), alkylcobalt complexes, alkyla- imidazole, 495 tion, 527 iodide complex, structure, 72 Grignard reagent: reaction with methylmagnesium iodide, cobalt(III) complexes, alkylation, 277, 278 517 see also Heptamethylcobyrinic acid phenyl(pyridine)cobaloxime, preparation, Heptamethylcobyrinic acid: 278 13Cnmr, 112 Group participation effects, f-amide cleavage, degradation, 113 235 ozonolysis, 115 Guanosine diphosphate: structure, 114 cobinamide phosphate, addition of, 151 Heptamethyl dicyano-5,15-bisnorcobyrinate: cobinamides nucleotide loop, biosyn thesis, preparation, 239

152 vitamin B 12, conversion to, 239 H2/Pt, reductive cleavage, methyl- Heptamethyl dicyano( 10-bromocobyrinate), cobalamin, 317 ozonolysis, 218 Hagemann's ester, vitamin B total syn thesis, 12 Heptamethyl dicyanocob yrinate: 184 preparation, 236 Haloenzyme synthetase, 163 reduction to heptanol, 226, 237 Halogen abstraction: vitamin B 12 , conversion to, 236 alkyl halides, cobalt(II) complexes, 519 Heterolytic cleavage: cobalt(II) complexes, 274 alkyIcobalamins, 305-319 electron transfer, bis(salicylaldehyde)- alkylcobaloximes, 305-319 ethylenediiminecobalt(II)- cobalt-carbon bond, vitamin B coenzyme, methylimidazole, 520 12 305-319,548

Hexacarboxylic acid (vitamin B12 ): Hydridocobalamin: bond angles, tables, 45-53 bond dissociation energy, 507 bond distances, tables, 45-53 electronic spectrum, 365 cell dimensions, 92 pKa values, 506 chemical formula, 92 preparation, 253, 365 deuteration, 212 secondary alkylcorrinoids, preparation, electronic spectrum, 417 552

folding, 60 vitamin B 12 coenzyme, 549 space group, 92 Hydridocobaloxime, 252 structure, 28, 204 Hydrido(pyridine)cobaloxime, bond torsion around A-D junction, 57 dissociation energy, 507 X-ray crystallographic data, 92 Hydrido(trwz-butylphosphine)cobaloxime: X-ray diffraction data, 27 bond dissociation energy, 507 X-ray structure, 31, 32 olefin addition, radical intermediates,

see also Vitamin B 12 518 Hexachloroiridate, oxidation, alkyl- pKa values, 506 cobaloximes, 515, table, 516 preparation, 253 5,7,7,12,14,14-Hexamethyl-l,4,8,ll- Hydridocobalt complexes: tetraazacyclotetradeca-4,11-diene- acidity, 253,506 cobalt: addition to olefins, mechanism, 265 alkyl complexes, 271 bond dissociation energy, 506 structure, 574 cobalt(I) complexes, equilibrium, 506

vitamin B 12 coenzyme, model systems, Hydridopentacyanocobalt: 574 acidity, 253 High pH, cob(II)inamides, epr spectrum, addition to olefins, mechanism, 263 447 bond dissociation energy, 507 High pressure liquid chromatography, olefin addition, free radical intermediates,

vitamin B 12 total synthesis, 190 518 Histidine cob(II)amide, epr spectrum pKa values, 506 simulation, 445 Hydrogen abstraction:

History, vitamin B 12, 1 5 '-deoxyadenosine, 554

Homocysteine: vitamin B12 coenzyme enzymic reaction, S-adenosylhomocysteine, from vitamin 554

B 12 coenzyme and, 298 Hydrogen cyanide, vitamin B 12 coenzyme methylation, methylcobalamin, 528 reaction with, 306 methylcobaloxime, me hylation, 529 Hydrogen exchange: Homolytic cleavage: with solvent, ribonucleotide reductase, cobalt-carbon bond: 449

activation enthalpy, 511 vitamin B 12 coenzyme enzymic reaction,

vitamin B12 coenzyme, 296, 362, 548 449 5-coordinate, 371 Hydrogen perox ide, corrin ox idation, 218 thermolysis, neopentylcobalamin, 364 Hydrogen reduc ion, cobaloximes, cobalt Hydrated electrons, reaction with corrin, complexes, 252 318 Hydrolysis: Hydrazines and oxygen: acid, amide groups (corrin periphery), cobaloximes, alkylation, 275 33,230,234 cobalt complexes, alkylation, 275 alkyl(pyridine)cobaloximes, cation

1,2-Hydride shift, vitamin B12 coenzyme, exchange resin, 249

549 Hydrophobic pocket, vitamin B 12 coenzyme. Hydrides: 41 cobalt, 365 Hydroxocobalamin: pK values, cobalt, 335 alkylation, vinyl ethers, 281 stability, cobalt, 335 electronic spectrum, 404, 417

Hydroxocobalamin (Cont'd) b-Hydroxy-n -propylpyridinatocobaloxime: initial isolation, 12 b-hydroxy-isopropylpyridinatocobaloxime, nmr spectrum, 468, 474 acid catalyzed rearrangement to, 314 nomenclature, 17 reaction with acid, 314 see also Aquocobalamin 4-Hydroxy-2,2,6,6-tetramethylpiperidine- Hydroxyalkylcobaloximes, reaction with N-oxylcobamide coenzyme, pre- acid, 313 paration, 267 2-Hydroxyalkylcobaloximes, preparation, Hyperfine splitting, epr spectroscopy, 436

reac ions, 284 Hypothetical pathways, vitamin B12 co- b-Hydroxyalkylcobaloximes, reaction with enzyme, enzymic reactions, 547 alkali, 310 a-Hydroxyalkylcobalt complexes, prepara tion, Imidazole, coordination to alkylcorrins, pulse readolysis, 273 358 4-Hydroxy-n-butylcobaloxime, reaction Imidazolecobalamin, electronic spectrum, with acid, 314 411 10-Hydroxycobalamin, 217 Incorporation into: trans-2-Hydroxycyclohexylcobaloxime, C tetanomorphum, sirohydrochlorin, reaction with alkali, 311 123 b-Hydroxye hylaquocobaloxime, decom- cobyric acid, trimethylated isobacterio- position in acid, 313 chlorins, 132 Hydroxyethylcobalamin: cobyrinic acid: acid decomposition, ethylene, 313 Factor I, 131 reaction with alkali, 311 sirohydrochlorin, 123 spin-lattice relaxation times, 492 corrin: 2-Hydroxyc hylcobaloximes: 5-aminolevulinic acid, 111 acid catalyzed decomposition, 518 methionine, 111 olefin p-complexes, acid catalysis, 575 porphobilinogen, 111 reaction with alkali, cob(I)aloxime, 310 15-cyano-l ,2,2,7,7,12,12-heptamethyl- Hydroxyethylcobinamide, reaction with corrin, metals, 211 alkali, 311 vitamin B12: Hydroxycthylcyanocobalamin, electronic cobalt, 211 spectrum, 413 copper, 211 2- Hydroxyethyl vinyl ether, reaction with rhodium, 211 cobalt(III) complexes, 282 zinc, 211 b-Hydroxyisopropylcobaloxime, reaction Infrared spectrum: with hydroxide, 310 lactones (corrin ring), 228 b-Hydroxyisopropyl(pyridine) cobaloxime: vitamin B12, 215 acid catalyzed rearrangement to 0-hydroxy- Inhibition: n -propylpyridinatocobaloxime, 314 nitrous oxide: photolysis, 302 diol dehydrase, 373 Hydroxylamine: e hanolamine ammonia-lyase, 373 acetylcobalamin, reaction with, 312 nitial isolation, hydroxocobalamin, 12 acetylglycobalamin, reaction with, 312 Insertion of dioxygcn, cobalt-carbon bond, glyglycobalamin, reaction with, 312 512 b-Hydroxypropionaldehyde, 328 Interaction with: b-Hydroxypropylcobaloximcs, acetone, corrin p-orbitals, cobalt orbitals, 561 photolysis, 302 corrin ring: b-Hydroxy-/i-propyl(pyridinc)cobaloxime, 5 '-deoxyadenosyl ligand, 66 preparation, 257 5,6-dimcthylbenzimidazole, 353 3- Hydroxy-rt -propylcobaloxime, reaction cosynthetase, uroporphyrinogen I, with acid, 314 118 |3-Hydroxy-H-propylcobaloximc, reaction substrate radicals, vitamin B 12r-, inter- with hydroxide, 310 mediate, 382

Interconversion: Isomerase reactions: cobalamin coenzymes, 163 basic schemes, 375 sirolactone, sirohydrochlorin, 123 carbonium ion mechanism, 377 Intermediate, enzymic reaction: epr spectroscopy, 381 vitamin B 12r, 381 neopentylcobalamin as model, 375 vitamin B 12 coenzyme, 5'-deoxy- proposed mechanisms, 383 adenosine, 332 vitamin B 12, dependent, table, 328, Intramolecular 1,2-shifts, organic radicals, 330-333 556 a,b-Isomers: Intramolecularly bridged cobaloximes, corrin, circular dichroism, 421 269 electronic spectrum, cobinamides, 413, Inversion of configuration, methionine table, 416 methyl transfer, 115 methylcobinamide, nmr spectroscopy Iodide: (13C), 484 heptamethylcob(II)yrinate, dimeric nmr spectrum, cyanoaquocobinamide, complex with, 522 484 vitamin B 12r, complex with, 522 Isopropylaquocobaloxime, redox potential, Iodine: 516 cleavage: Isopropyl bis(acetylacetone)ethylenediimine- me hylcobalamin, 316 cobalt, radical scavengers, thermal stereochemistry, (S)-me hylheptyl- decomposition, 512 pyridinatocobaloxime, 317 Isopropylbis(salicylaldehyde)ethylenediimine- vitamin B 12 coenzyme, 316 cobalt, radical scavengers, thermal lactone formation, vitamin B12, 226 decomposition, 512 Iodocobalamin, electronic spectrum, 411 Isopropyl bis(salicylaldehyde-o - phenylene- Iodocobalt(II) [cobyrinic acid-a,b,c,d,e,f,g- diimine)cobalt, radical scavengers, heptamethyl ester] dimer: thermal decomposition, 512 cell dimensions, 95 Isopropylcobalamin: chemical formula, 95 electronic spectrum, 255, 408 space group, 95 b-elimination, vitamin B128 , 364 X-ray crystallographic data, 72, 95 pH decomposition rates, 370 Ion exchange chromatography, corrin, rate of acid catalyzed decomposition, 249 371 Ionization energies, metals, 331 thermolysis: Iron alkyl bond, 331 base-on, off, 552 7-Irradiation, frozen solution: kinetics, 552 vitamin B 12, 318 Isopropylcobaloxime: vitamin B 12 coenzyme, 318 cobalt-carbon bond: 3-Isoadenosylcobalamin, acid cleavage, bond dissociation energy, 511 312 length, 359 Isobacteriochlorins: halogen cleavage, 317 sulfite and nitrite reductases, 122 Isopropylcobinamide, electronic spectrum, synthesis, 122, 135 temperature variation, 255, 348, see also Sirohydrochlorin; Sirolactone 408 Isolation: 2', 3 -Isopropylidcneadenosylcobalamin C tetanomorphum, Factor I, 130 and r-butoxide, vitamin B 128 , 307 corriphyrin-3, 134 2',3'-O-Isopropylidenecy clodihydrouridine: corriphyrins, 121, 122 formation, 297 desulfoviridin, sirohydrochlorin, 122 structure, 298 P. Shermanii Factor I, 130 t 2', 3 '-Isopropylidene-5 '-deoxy-(D)ribosyl- sirohydrochlorin, P. shermanii, 122 cobinamide, nmr spectrum, 486 trimethylated isobacteriochlorins, 132 2', 3 '-O-Isopropylidene-5 '-deoxy-8,5 '- vitamin B 12, 3, 24 cyclonucleosides, 300

2', 3'-O-Isopropylidene-5 '-deoxyuridyl- halogenation, 226 cobalamin, photolysis, 297 methylcobalamin, 226 Isopropyl(pyridine)bis(salicylaldehyde-o- sulfonatocobalamin, 226 phenylenediimine)cobalt, bond vitamin B 12, 225, 234

dissociation energy, 512 vitamin B 12 coenzyme, 226 Isopropyl(pyridine)cobaloxime, cobalt- Lactams (corrin ring): carbon bond, bond lengths, 505 biological activity, 225

Isopropyl(tricyclohexylphosphine) cobaloxime: electronic spectrum, vitamin B12 , 417 cobalt-carbon bond, bond leng hs, 506 formation, mechanism, 226 nmr spectrum, 506 c-lactam forma tion, 23 4 Isopropy l(triphenylphosphine) cobaloxime: Lactobacillus leichmanni: cobalt-carbon bond, bond leng hs, 505 cobalamin biosynthesis, 160

nmr spectrum, 506 ribonucleotide reductase, vitamin B nr

Isotropic exchange, epr spectroscopy, formation, 439 452 Lactone formation:

Isoxazoles, vitamin B 12 total synthesis, 175 corrin, cyclization (peripheral), 225-230 halogenation, 226 Kinetic isotope effect: iodine, 226 2 [I- H2 ] propane-l,2-diol, vitamin B12 vitamin B 12, 226 coenzyme, 554 Lactones (corrin ring):

vitamin B12 coenzyme, enzymic reaction, electronic spectrum, vitamin B12, 417 554 infrared spectrum, 227 Kinetics: mechanism of forma ion, 225-230 cobaloximes, alkylation, 259 preparation, 226 cobalt-carbon bond: spiro, 227 activation en halpy, 511 Lanthanide shift reagents: dissociation energy determination, corrin ring, nmr spectrum, 471, 482 511 nmr spectrum, carboxymethylcobalamin, cobalt(I) complexes, alkylation, 258 472 cyclopropylcarbinyl radical rearrange ments , 567 Laser Raman spectrum, corrin derivatives, isopropylcobalamin thermolysis, 552 343 vitamin B 12s alkylation, 259 LCAO-MO, electronic spectrum, 396 Kramer's doublets, 435 Lead(II): alkylation, trans-dimethylcobalt(III) 13C-Labelled: complexes, 527 alkylcobalamins, 268 cobalt-carbon bond, 54 cobalamins, 474 a-Leucine, (R)-2,5-diaminopentanoate, corrin, 474 546 2 H-Labelled, vitamin B 12 coenzyme, 5'- LiAIH4, heptamethyl dicyanocobyrinate methylene group, 545 reduction, 237 3 H-Labelled, vitamin B 12 coenzyme, 5'- Ligand binding, vitamin B 12 coenzyme methylene group, 545 model systems, 504

Labilization by: Ligand equilibria, vitamin B12 coenzyme protein, cobalt-carbon bond, 333 steric effects, 341 steric interactions, cobalt-carbon bond, Ligand exchange: 361 alkylcobalamins, steric effects, 341 Lack of aromaticity, corrin, 204 5 ,6-dimethylbenzimidazole, thermo- Lactam formation: dynamics, 496 corrin, cyclization (peripheral), 225-230, Ligand modification, alkylcobalt complexes, 234 283-286 Ligand ordering, trans-effect, 346 Ligand substitution: corrin, 330, 337

Ligand substitution (Cont'd) enzymic reaction, ethanolamine ammonia-

equilibrium constants, table, aquo- lyase, vitamin B 12 ,.-substrate radical cobalamin, 337 separation, 453 Ligands, s-donor power, 333 hydridocobalt complexes, addition to Lithium, incorporation into 15-cyano- olefins, 265 1,2,2,7,7,12,12 -heptamethyl- hydridopentacyanocobalt, addition to corrin, 21 i olefins, 263

Longitudinal relaxation times, vitamin B12 , lactams (corrin ring), formation, 225 nmr spectrum, 485 methionine, methyl transfer, 113 Loss of C-20 in corrin biosynthesis, 137 model systems, 383

Low spin Co(II), vitamin B 12r , 432 olefins, addi ion to cobalt(I) complexes, Luminescence: 262 cobalt-free, corrinoid, 426 reductive alkylation, cobalt complexes, corrin, 426 254-270

vitamin B 12,426 role of model systems, vitamin B 12 D-a-Lysine, 328 coenzyme, 528 L-b-Lysine, 328 vitamin B 12 coenzyme, methylmalonyl-CoA mutase, 565 Macrocycle reactions, corrin, 201-243 Mechanism of ac ion: Magentic circular dichroism: model systems, vitamin B12 coenzyme, cobalt 15-cyano-7,7,12,12,19-penta- 543-582 methylcorrin, 424 theory, vitamin B12 coenzyme, 543-582 cobalt-free corrin, 423 Mechanism of formation: cob(II)inamides, 426 dehydrocobinamide, 226 copper cobalamin, 426 yellow corrinoids, 39, 229 dicyanoheptamethylcobyrinate, 426 Me[14]-diene N4: metallocorrins, 424 pulse radiolysis, 574 nickel 15 - cy ano - 7,7,12,12,19 - pen ta- structure, 574 methylcorrin, 424 Mercaptides: nickel 7,7,12,12,19 -pentamethylcorrin alkylcobaloximes, reaction with, 311 , 424 methyl(aquo)cobaloxime, reaction with Magic Mannich, dimethylaminomethylation 311 of corrin, 213 Mercury(II): Magnetic properties, corrin, 330 alkylation: Malononitrile, reaction with cobalt(III) alkylcobaloximes, 526 complexes, 279 alkylcobalt complexes, 526 Mammalian: methylpentacyanocobaltate(III), 5 26 biosynthesis, methylcobalamin, 163 cobalamins, coordination, 495 methionine synthetase, 163 cobalt-carbon bond cleavage, 526 MCD, see Magnetic circular dichroism methylation, methylcobalamin, 529 Me6[14]diene N4,see 5,7,7,12,14,14- methylcobalamin alkylation, 526 Hexamethyl-1,4,8,11 -tetraaza- methylpentacyanocobalate(III), 529 cyclotetradeca-4,11-dienecobalt; stereochemistry, alkylcobalt complexes, Cobalt complexes 526 Mechanism: Meso-substitution, corrin, 212 alkynes, addition, 263 Metal complexes, secocorrins, X-ray crystal- carbon-skeleton, 385 lographic data, 77, 96 cobaloximes, addition to olefins, 264 Metal-free: cobalt complexes, reductive arylation electronic spectrum, corrin, 207, 395 electron transfer, 270 vitamin B 12, 211 cobalt(I) complexes, addition to Metal ions: olefins, 265 adenosyla ing enzyme, 161 corrin epimerization, 220 cobalamins, reaction with, 495

Metallation: Methoxycarbonylethylcobalamin, reaction corrin, 210-212 with alkali, 310 15-cyano-l,2,2,7,7,12,12-heptamethyl- Methoxyethylcobalamin ethylene, acid corrin, 211 decomposition, 313 descobaltocobalamin, 211 Methylacrylate, addition to cobalt(I) descobaltocobamide, 211 complexes, 256 15 -cy ano -1,2,2,7,7,12,12 - heptamethyl- Methyl(aquo)cobaloxime: corrin, 211 cobalt-carbon bond, bond lengths, 505 Metal-Iigand bond angles, 46 methane formation, hydroxide, 308 Metal-Iigand bond lengths, 45 photolysis, acetaldehyde, 571 Metallocorrins: reaction with: deuteration, 220 acid, 313 electronic spectrum, 424 mercaptides, 311 magnetic circular dichroism, 424 redox potential, 516 Metalloenzyme chemistry, 326 Methyl(aquo)cobyrinic hepta terf-alcohol: Metalloporphyrins, cobalt-carbon bond, preparation, 278 246 structure, 278

Metal replacement, vitamin B 12 , 72 threo-b-Methylaspartic acid, 328 Metals: Methylation: ionization energies, 331 homocysteine, methylcobaloxime, 529 methylation, methylcobalamin, 528 methylcobalamin: Methane biosynthesis, methylcobalamin, homocysteine, 528 528 mercury(II), 529 Methane formation, hydroxide and metals, 528 5 methyl(aquo)cobaloxime, 308 N methyltetrahydrofolic acid, vitamin B12

Methanolysis, vitamin B12, 236 528 Methanosarcina barkeri, methylcobalamin stereochemistry, methionine, 113 biosynthesis, 162 1-Methylbilane, corrin biosynthesis, 121 Methionine: 2- Mehyl-2-butylcobalamin, rate of, 371 biosynthesis: 1-Methylbut-3-enyl(pyridine)cobaloxime,

FMNH2 , 162 rearrangements,2-methylbut-3- NADPH, 162 enyl(pyridine)cobaloxime, 569 chiral methyl, 115 2- Methylbut-3-enyl(pyridine)cobaloxime, incorporation into: 1-methylbut-3-enyl(pyridine)- corrin, 111 cobaloxime, rearrangements, 569 13C, 112 Methylcobalamin: methylation, stereochemistry, 113 alkylation, mercury(II), 526 methyl transfer: biosynthesis: inversion of configuration, 115 Clostridium thermoaceticum, 161

mechanism, 113 E. Coli f 161 Methionine formation, S-adenosyl- Methanosarcina barkeri, 162 methionine, 329 NADPH, 162 Methionine synthetase: Streptomyces griseus, 161-163 activation, 162 carbon dioxide, reduction to, 528 mammalian, 163 circular dichroism, 420 13 [ CH 3 ]-L-Methionine: complex with, Z>w-acetylacetone-

vitamin B12 biosynthesis, 480 ethylenediamine, X-ray structure,

CD 3 -methyl incorporation into: 349 corrin, 114 13C containing, 268, 301, 326

I ntact transfer, 114 conversion to vitamin B 12 coenzyme, 8-Methoxyadenosylcobalamin, 298 163 5-Methoxybenzimidazole, Factor III, coupling constants 13C-H, 490 471 dimcthylmercury(II), 526

13 Mcthylcobalamin (Cont'd) nmr spectroscopy ( C), a, j3-isomers, electrochemical oxidation, 517 484 electrochemical reduction, 318 Methylcorrinoids: electronic spectrum, 408, 415 trans-effect, nmr spectroscopy, 489 enzymic reaction, 528 a ,b, photoisomerization, 301 flash photolysis, 300, 335, 363, 525, Methylcyanocobalamin: 553 electronic spectrum, 413 H2/Pt, reductive cleavage, 317 nmr spectrum, 468 halogenation, 216 3-Methylcyclopropylcarbinyl(pyridine)- heavy metals, 528 cobaloxime rearrangements, 1- homocysteine, methylation, 528 methyl-but -3-enyl(pyridine)- iodine, cleavage, 316 cobaloxime, 569 lactam formation, 226 l-Methyl-2,2-diphenylcyclopropyl- mammalian, biosynthesis, 163 (pyridine)cobaloxime prepara- mercury(Il), methylation, 529 tion, 254 metals, methylation, 528 N-Methyleneaniline(pyridine)cobaloxime methane, biosynthesis, 528 preparation, 258 methyl transfer, thiols, 312 a-Methyleneglutarate mutase: monomethylmercury(II), 526 model systems, vitamin B12 coenzyme, nmr spectrum: 567 pH dependence, 494 radical intermediates, 557 praseodymium, 471, 474, 483 reaction pathways, vitamin B 12 coenzyme, nomenclature, 21 570 photolysis: a-Methyleneglutaric acid, 328 ethane, 300 a-Methylene mutase, model systems, 532 methyl radicals, 300 1-Methyl-heptylcobaloxime, cobalt-carbon

vitamin B 12r, 300, 362,404 bond, bond dissociation energy, rate of decomposition, 368 511 reaction with methylmercaptide, 311 (S)-Methylheptylpyridinatocobaloxime, spin-lattice relaxation times, 492 iodine cl eavage, ste reochemistry, thermolysis, 303, 363 317

vitamin B 12 coenzyme: Methylisocyanatocobalamin, electronic conversion to, 163 spectrum, 411 ratio, 161 b-Methylitaconic acid, 328 see also Alkylcobalamins; Alkylcorrins; Methylmagnesium iodide, heptamethyl- Cobalt-carbon bond cobyrinate reaction with, 278 Methylcobaloxime: L-Methylmalonyl-CoA, 328 cob(II)aloximes, photolysis, 301 Methylmalonyl-CoA mutase: cyanide, acetonitrile formation, 307 carbanion intermediates, 556 flash photolysis, 405 enzymic reaction, 546 methyla ion, homocysteine, 529 mechanism, vitamin B 12 coenzyme, nmr spectrum (59Co), 490 565 photolysis, methylperoxocobaloxime, MO-calculations, 557 301,553 model systems, vitamin B 12 coenzyme, see also Methyl(aquo)cobaloxime 532,564 Methylcobalt complexes: reaction pathways, vitamin B 12 co- bond lengths, nmr spectroscopy, 506 enzyme, 565,566 flash photolysis, 525 vitamin B 12 coenzyme, enzymic reac- Methylcobinamidc: tion, 529 electrochemical reduction, 318 Methylmercaptide, methylcobalamin electronic spectrum, temperature varia- reaction with, 311 tion, 343, 348,408 Methylmercury isopropoxide, vitamin B12 13C-enriched, 484 total synthesis, 185

Methylpentacyanocobalate(III), mercuric Model systems: chloride alkylation, 526 bis(salicylaldehyde)ethylenediimine-

Methylperoxocobaloxime, methylcobaloxime cobalt, vitamin B12 coenzyme, photolysis, 553 551 l-Methyl-2-phenylethylcobaloxime, cobalt- cobalt role, 378 carbon bond, bond dissociation diol dehydrase, 532

energy, 511 ligand binding, vitamin B12 coenzyme, Methyl(pyridine)bis(acetylacetone)- 504 ethylenediiminecobalt, cobalt- mechanism, 383 carbon bond, bond lengths, methylmalonyl-CoA mutase, 532

505 pKa values, vitamin B 12 coenzyme, Methyl(pyridine)cobaloxime, cobalt-caxbon 504

bond, bond lengths, 505 redox chemistry, vitamin B 12 coenzyme, Methyl radicals: 504

methylcobalamin photolysis, 300 redox potential, vitamin B 12 coenzyme, reactions, 300 504

recombination: vitamin B 12 : cob(II)alamin, 511 comparison to, 504 with cobalt(II) complexes, 335 redox chemistry, 513

vitamin B12r, 553 vitamin B 12 coenzyme: scavenger, vitamin B ur, 300 alkylcobalt complexes, 551, 564 N5 -methyltetrahydrofolic acid, vitamin aminomutases, 571 B 125 methylation, 528 bis(salicylaldehyde)ethylenediimine- Methyl transfer: cobalt(III), 551 Inversion of configuration, methionine, capped cobaloximes, 533, 565 115 cobalt-carbon bond cleavage, 551 mechanism, methionine, 113 comparison to, 504 thiols, methylcobalamin, 312 diol dehydrase, 571 Methyltransferase enzyme: enzymic reaction, 501-541, 564-577 properties, 135 ethanolamine ammonia-lyase, 571 purification, 135 glutamate mutase, 570 Methyl(triphenylphosphine) cobaloxime, mechanism, role of, 528 cobalt-carbon bond, bond lengths, mechanism of action, 543-582 505 a-methyleneglutarate mutase, 377, Microbiological assay, vitamin B 12, 7 501-541,567 Microbiological formation, yellow methylmalonyl-CoA mutase, 564 corrinoids, 228 redox chemistry, 513 Migration of group X, electron transfer, Modified cobalamins, cobalt-carbon bond vitamin B 12 coenzyme, 555 cleavage, 65 MO-calculations: Molecular orbitals, bridged cation, 555 aminomutases, 557 p-Molecular orbitals, corrin, 397 corrin: Molecular rearrangements, vitamin B 12 electrophilic substitution, 212 coenzyme, 545 epimerization, 220 Molecular structure in solution, com parison diol dehydrase, 557 to X-ray structure by ethanolamine ammonia-lyase, 557 nmr spectroscopy, 482 methylmalonyl-CoA mutase, 557 Mono-C-methylated chlorin, structure, vitamin B 12 coenzyme, enzymic 131

reac ion, 557 Monocarboxylic acid, vitamin B 12: vitamin B 12, electrophilic attack, 212 bond angles (tables), 45-53 Model for corrin, cobaloximes, 419 bond distances (tables), 45-53 Model for ethanolamine ammonia-lyase, cell dimensions, 93 vitamin B 12 coenzyme photolysis, 196 chemical formula, 93

13 Mcthylcobalamin (Cont'd) nmr spectroscopy ( C), a,0-isomers, electrochemical oxidation, 517 484 electrochemical reduction, 318 Methylcorrinoids: electronic spectrum, 408, 415 trans-effect, nmr spectroscopy, 489 enzymic reaction, 528 a,|b, photoisomerization, 301 flash photolysis, 300, 335, 363, 525, Methylcyanocobalamin: 553 bbelectronic spectrum, 413 H2/Pt, reductive cleavage, 317 bbnmr spectrum, 468 halogenation, 216 3-Methylcyclopropylcarbinyl(pyridine)- heavy metals, 528 cobaloxime rearrangements, 1- homocysteine, methylation, 528 methyl-but -3-enyl(pyridine)- iodine, cleavage, 316 cobaloxime, 569 lactam formation, 226 l-Methyl-2,2-diphenylcyclopropyl- mammalian, biosynthesis, 163 (pyridine)cobaloxime prepara- mercury(Il), methylation, 529 tion, 254 metals, methylation, 528 N-Methyleneaniline(pyridine)cobaloxime methane, biosynthesis, 528 preparation, 258 methyl transfer, thiols, 312 a-Methyleneglutarate mutase: monomethylmercury(II), 526 model systems, vitamin B 12 coenzyme, nmr spectrum: 567 pH dependence, 494 radical intermediates, 557 praseodymium, 471, 474, 483 reaction pathways, vitamin B 12 coenzyme, nomenclature, 21 570 photolysis: a-Methyleneglutaric acid, 328 ethane, 300 a-Methylene mutase, model systems, 532 methyl radicals, 300 1 -Me hyl-heptylcobaloxime, cobalt-carbon

vitamin B 121., 300, 362,404 bond, bond dissociation energy, rate of decomposition, 368 511 reaction with methylmercaptide, 311 (S)-Methylheptylpyridinatocobaloxime, spin-lattice relaxation times, 492 iodine cl eavage, ste reochemistry, thermolysis, 303, 363 317

vitamin B 12 coenzyme: Me hylisocyanatocobalamin, electronic conversion to, 163 spectrum, 411 ratio, 161 b-Methylitaconic acid, 328 see also Alkylcobalamins; Alkylcorrins; Methylmagnesium iodide, heptamethyl- Cobalt-carbon bond cobyrinate reaction with, 278 Methylcobaloxime: L-Methylmalonyl-CoA, 328 cob(II)aloximes, photolysis, 301 Methylmalonyl-CoA mutase: cyanide, acetonitrile formation, 307 carbanion intermediates, 556 flash photolysis, 405 enzymic reaction, 546 methyla ion, homocysteine, 529 mechanism, vitamin B 12 coenzyme, nmr spectrum (59Co), 490 565 photolysis, methylperoxocobaloxime, MO-calculations, 557 301,553 model systems, vitamin B 12 coenzyme, see also Mcthyl(aquo)cobaloxime 532,564 Methylcobalt complexes: reaction pathways, vitamin B 12 co- bond lengths, nmr spectroscopy, 506 enzyme, 565,566 flash photolysis, 525 vitamin B 12 coenzyme, enzymic reac- Methylcobinamidc: tion, 529 electrochemical reduction, 318 Methylmercaptide, mcthylcobalamin electronic spectrum, temperature varia- reaction with, 311 tion, 343, 348,408 Methylmercury isopropoxide, vitamin B12 13C-enriched, 484 total synthesis, 185

Methylpentacyanocobalate(III), mercuric Model systems: chloride alkylation, 526 bis(salicylaldehyde)ethylenediimine-

Methylperoxocobaloxime, methylcobaloxime cobalt, vitamin B12 coenzyme, photolysis, 553 551 l-Methyl-2-phenylethylcobaloxime, cobalt- cobalt role, 378 carbon bond, bond dissociation diol dehydrase, 532

energy, 511 ligand binding, vitamin B 12 coenzyme, Methyl(pyridine)bis(acetylacetone)- 504 ethylenediiminecobalt, cobalt- mechanism, 383 carbon bond, bond lengths, methylmalonyl-CoA mutase, 532

505 pKa values, vitamin B 12 coenzyme, Methyl(pyridine)cobaloxime, cobalt-carbon 504

bond, bond lengths, 505 redox chemistry, vitamin B 12 coenzyme, Methyl radicals: 504

methylcobalamin photolysis, 300 redox potential, vitamin B 12 coenzyme, reactions, 300 504

recombination: vitamin B 12: cob(II)alamin, 511 comparison to, 504 with cobalt(II) complexes, 335 redox chemistry, 513

vitamin B12r, 553 vitamin B 12 coenzyme: scavenger, vitamin B 121 ., 300 alkylcobalt complexes, 551, 564 N5 -methyltetrahydrofolic acid, vitamin aminomutases, 571 B 12s methylation, 528 bis(salicylaldehyde)ethylenediimine- Methyl transfer: cobalt(III),551 inversion of configuration, methionine, capped cobaloximes, 533, 565 115 cobalt-carbon bond cleavage, 551 mechanism, methionine, 113 comparison to, 504 thiols, methylcobalamin, 312 diol dehydrase, 571 Methyltransferase enzyme: enzymic reaction, 501-541, 564-577 properties, 135 ethanolamine ammonia-lyase, 571 purification, 135 glutamate mutase, 570 Methyl(triphenylphosphine)cobaloxime, mechanism, role of, 528 cobalt-carbon bond, bond leng hs, mechanism of action, 543-582 505 a-methyleneglutarate mutase, 377, Microbiological assay, vitamin B 12, 7 501-541,567 Microbiological formation, yellow methylmalonyl-CoA mutase, 564 corrinoids, 228 redox chemistry, 513 Migration of group X, electron transfer, Modified cobalamins, cobalt-carbon bond vitamin B 12 coenzyme, 555 cleavage, 65 MO-calculations: Molecular orbitals, bridged cation, 555 aminomutases, 557 pr-Molecular orbitals, corrin, 397 corrin: Molecular rearrangements, vitamin B 12 electrophilic substitution, 212 coenzyme, 545 epimerization, 220 Molecular structure in solution, comparison diol dehydrase, 557 to X-ray structure by ethanolamine ammonia-lyase, 557 nmr spectroscopy, 482 methylmalonyl-CoA mutase, 557 Mono-C-methylated chlorin, structure, vitamin B 12 coenzyme, enzymic 131

reaction, 557 Monocarboxylic acid, vitamin B 12: vitamin B 12, electrophilic attack, 212 bond angles (tables), 45-53 Model for corrin, cobaloximes, 419 bond distances (tables), 45-53 Model for ethanolamine ammonia-lyase, cell dimensions, 93 vitamin B 12 coenzyme photolysis, 196 chemical formula, 93

Monocarboxylic acid, vitamin 7 C-13 epimer, 33 space group, 93 cell dimensions, 93 structure, 34 chemical formula, 93

torsion around A-D junction, 57 comparison to vitamin B12, 35 X-ray crystallographic data, 93 conformations, 209 see also Vitamin B12 folding, 60 Monocarboxylic acid (E2), 83 nmr spectrum, 485 Monoclinic model, vitamin B 12r, epr planarity deviations, 61 spectroscopy, 439 space group, 93 Monolactone, see Sirolactone structure, 34, 224 Monomethylmercury(II), methylcobalamin, torsion around A-D junc ion, 57 526 X-ray crystallographic data, 93 Mutase reactions, vitamin B12 dependent, X-ray structure, diagram, 34, 36 table, 328 see also 13-Epicorrinoids Nephelauxetic series: NADH, cobalamin reduction, 157 electronic spectrum, 409 NADPH: trans-effect, 336 methionine biosynthesis, 162 Neurological abnormalities, pernicious methylcobalamin biosynthesis, 162 anemia, 2 Neocobalamins, pK values, steric effects, Neutron diffraction:

489 VitaminB12 coenzyme, 91

Neocobinamide, 232, 234. See also vitamin B 12 , monocarboxylic acid (E2), Neocorrinoids 33 Neocobyric acid, total synthesis, 187, Nickel corrin: 196,232 bond distances, angles, tables, 45-53 Neocorrinoids: folding, 60 chromatography, 222 planarity, devia ions, 61 circular dichroism, 222, 225 torsion around A-D junction, 57 electronic spectrum, 222 Nickel 1,19 -dimethyloctadehydrocorrin, 3-epicorrinoids, 224 catalytic, reduction, 238 8-epicorrinoids: Nickel 7,7,12,12,19-pentamethylcorrin: biological activity, 225 electronic spectrum, 424 circular dichroism, 224 magnetic circular dichroism, 424 13-epicorrinoids, 221 Nickel(II) 5-cyano-l6-ethoxy-1,8,8,13,13- epimerization, 220 pentamethyl-14-methylene-CD- optical rotatory dispersion, 222 secorrin perchlorate: trifluoroacetic acid, epimerization, 222 cell dimensions, 96 see also 3-Epicorrinoids; 8-Epicorrinoids; chemical formula, 96

13-Epicorrinoids; NeovitaminB 12 space group, 96 Neopentylcobalamin: X-ray diffraction data, 96 homolytic cleavage, thermolysis, 364 Nickel(II) 15 - cy ano -2,2,7,7,12,12- isomerase reactions, 375 hexamethyl- 1-methylene-AD- rate of decomposition, 368 secocorrin perchlorate: thermolysis, 552 cell dimensions, 96 Neopentyl(pyridine)bis(salicylaldehyde- chemical formula, 96 o-phenylenediimine)cobalt, bond space group, 96 dissociation energy, 512 X-ray diffraction data, 96 Neophyl rearrangement, organic radicals, 556 Nickel(II) 15 -cyano -7,7,12,12,19-

Neovitamin B 12: pentamethylcorrin chloride, biological activity, 224 conformations, 208 bond angles, tables, 45-53 Nickel 15 - cyano -7,7,12,12,19 - penta- bond distances, tables, 45-53 methylcorrin: electronic spectrum, 424

Nickel 15-cyano-7,7,12,12,19-pentamcthyl- cobalt-carbon bond, polarizability, corrin {Cont'd) 489 magnetic circular dichroism, 424 cobalt complexes: Nickel(II)-1,2,2,7,7,12,12- cis-effect, 487 heptamethyl-15 -cy ano-1,19- trans-effect, 488 epoxysecocorrin perchlorate: cobalt(I) complexes, 486 cell dimensions, 97 cobalt(II) complexes, 486 chemical formula, 97 corrin: space group, 97 cis-effect, 487 X-ray diffraction data, 97 trans-effect, 463-500 Nickel(II) -1,2,2,7,7,1212 -heptamethyl - 5,6 -dimethylbenzimidazole: 15-cyano-18-dehydrocorrin: protonation, 494 cell dimensions, 97 trans-effect, 488 chemical formula, 97 electronic structure, corrinoids, 487 space group, 97 fluxionality, cobalamins, 490 X-ray diffraction data, 97 methylcobalt complexes, bond lengths, Nickel(II) 1,8,8,13,13 -pentamethyl-5 - 506 cyano -trans-cou'm chloride: methylcorrinoids: cell dimensions, 95 13C containing, 484 chemical formula, 95 trans-effect, 489 space group, 95 molecular structure in solution, X-ray crystallographic data, 95 comparison to X-ray structure, Nico inate mononucleotides: 482 cobalamins, biosynthesis, 153 nuclear Overhauser effect, 479 deamidation, 153 pH dependence, cobalamins, 493

Nitrile hydrolysis, vitamin B 12 total structural information, 482 synthesis, 191 temperature dependence, cobalamins, Nitroalkylcobalamin photolysis, 405 490

Nitroalkylcobinamide photolysis, 405 vitamin B12 biosynthesis, 479

Nitroalkylcorrins photolysis, epr vitamin B12 coenzyme, 465 spectrum, 405 Nmr spectrum: Nitromethane: aquocobalamin, 468 cobalt alkylation, 280 13C, biosynthetic studies: reaction w ith a quohydroxo Co(III), 336 dicyanocobalamin, 112

Nitrosation: vitamin B12, 112,480 corrin, 217 13 CN-enriched, dicyanocobalamin,

vitamin B 12, 217 478 10-Nitrosocobalamin: C-0 proton, corrin ring, 469 electronic spectrum, 217 carboxymethylcobalamin, lanthanide nomenclature, 17 shift reagents, 472 preparation, 217 chemical shifts:

Nitrosodurene, reaction with vitamin B12 vitamin B 12,485 coenzyme, 298 vitamin B 12 coenzyme, 465 Nitrosyl chloride, reaction with corrin, cobalamins, table, 474 217 cobaloximes, 247

Nitrous oxide: corrin ring, vitamin B 12 coenzyme, diol dehydrase inhibition, 373 469 ethanolamine ammonia-lyase inhibition, corriphyrin-3, 135 373 coupling constants, table, 484 Nitroxidcs, spin-trapped, 298 cyanoaquocobinamide, a )3-isomers, Nmr spectroscopy: 484

biosynthetic studies, 486 5 '-deoxyadenosyl ligand, vitamin B 12 cobalamins, isomeric forms, 463-500 coenzyme, 468, 477

Nmr spectrum (Cont'd) vitamin B 12r, paramagnetic shifts, 487 13 dicyanocobalamin (table), ( C), 476 vitamin B 12s, 486 dicyanocobinamide, table, (13C), 476 yellow corrinoids, 229, 485

5,6-dimethylbenzimidazole, vitamin B 12 Noble prize, vitamin B 12 , 2 coenzyme, 468, 477 Nomenclature, vitamin B 12 and derivatives, ethylcobalamin, 468, table, 474 17-22 Factor 111,471,472 1 -Norbornyl(pyridine)cobaloxime, pre paration, 1 H/ 2H exchange, corrin ring, 469 255 hydroxocobalamin, 468, table, 474 2-Norbornylcobalamin, rate of decomposi tion, 2-3 '-isopropylidene-5 '-deoxy-0 (D)- 368 ribosylcobinamidc, 486 Nuclear Overhauser effect: isopropyl(tricyclohexylphosphine) nmr spectroscopy, 479 cobaloxime, 506 sirohydrochlorin, octamethyl ester, nmr isopropyl(triphenylphosphine) cobaloxime, spectrum, 125 506 Nucleophilic attack: lanthanide shift reagents, corrin ring, cobalt-carbon bond cleavage, 527 471,482 cobalt(III) complexes, 284 Nucleophilic displacement, R+ from longitudinal relaxation times, vitamin B12 , + 485 (alkylcobalt) ,516 Nucleophilicity: methylcobalamin, 471, table, 474 bis(salicylaldehyde)ethylenediimine- methylcobaloxime, 490 cobaltcomplexes, 523 methylcyanocobalamin, 468 cob(I)aloximes, 523 neovitamin B 12, 485 cob(I)inamide, 250, 251 nuclear Overhauser effect, siiohydro- cobalt(I) complexes, table, 251 chlorin, oct amethyl e ster, 1 23 definition, 250 paramagnetic sh ifts, cor rin ring, 471 diacetylmonoximeimino diacetylmono- pH, dependence, methylcobalamin, ximatoiminopropane-l,3-cobalt(I), 494 523 praseodymium: effect of axial ligands, cobalt(I) complexes, aquocobalamin, 483 252 methylcobalamin, 483 vitamin B 12s , 251, 523 vitamin B 12,484 Nucleoside analogs, vitamin B12 coenzyme, vitamin B coenzyme, 483 12 160 propanolamine, vitamin B12 coenzyme, Nucleosides, conformations, table, 70 467 Nucleoside triphosphates: protonated, vitamin B coenzyme, 468 12 adenosylating enzyme, 160 ribosc ring, vitamin B12 coenzyme, 467, adenosylation, C. tetanomorphum, table, 478 160 side chain, corrin ring, 480 Nucleotide loop: sirolactone, hcptamethyl ester, 123 acid hydrolysis, 234 trimethylated isobacteriochlorins, 132 biosyn hesis: vinylcobalamin, 490 [R] -l-amino-2-propanol, 149 vitamin B 12: cobalamins, 148 (13C) table, 476 corrin, 148 monocarboxylic acid, 471, 486 glutathione, 152 vitamin B coenzyme: 12 guanosine diphosphate, 152 5'-2H-deoxyadenosyl ligand, 471 Propionibacterium arabinosum, 1HZ2H exchange, 468, 469 152 protonated, 468 13 biosynthetic scheme, 149 VitaminB12 coenzyme ( C), table, conformations, 65 476 reactions, 234-236 vitamin B 12 coenzyme, table, 474 Nucleotides, conformations, table, 70 vitamin B 12, table, 474

Numbering, vitamin B 12 and derivatives, pentacyanocobaltate, reaction with, nomenclature, 18 276 One-electron oxidation, alkylcobalamins, Octadehydrocorrin, nomenclature, 19 515,517 Octamethyl ester: Optically active alkyl ligands, cobaloximes, electronic spectrum, sirohydrochlorin, 268 123 Optical rotatory dispersion: nmr spectrum, nuclear Overhauser effect, neocorrinoids, 222

sirohydrochlorin, 123 vitamin B12, 223 sirolactone, 122 Orbital energies: trimethylated isobacteriochlorin electronic corrin, 206, 399

spectrum, 132 vitamin B12, 206 2,2,7,7,12,13,17,18-Octame hylisobacterio- Orbitals, cobalt(II) complexes, 438, 440 chlorin: Orbital symmetry, vitamin B12 total structure, 136 synthesis, 176 synthesis, 136 Organic radical interaction: Olefin addition: epr spectrum: cob(I)aloximes, alkylation, 523 cobalt(II) complexes, 450 cobalt(I) complexes, alkylation, 523 enzymic reaction, vitamin B12r, 450 free radical intermediates, hydridopenta- separation, vitamin B 121 ., 452 cyanocobalt, 518 Organic radical recombination, vitamin radical intermediates, hydrido(tri-n- B12r rate, 525 butylphosphine)cobaloxime, 518 Organic radicals: p- Olefin complexes: cobalt(II) complexes, reaction with, 2-acetoxyalkylcobaloximes, 575 271 acid catalysis: enzymic reaction, epr spectroscopy, 2-hydroxyethylcobaloxime, 575 559 phenacylcobalamin, 575 intramolecular 1,2-shifts, 556 cob(III)aloxime, 314 neophyl rearrangement, 556 cobalt(I) complexes, acrylonitrile, 527 rearrangements, role of cobalt, 531, 533, cobalt(III) complexes, 282 556 1,2-dihydroxyethylcobalt, 574 vitamin B 12 coenzyme, enzymic reac tions, 2,2-dihydroxyethylcobalt, 574 545, 547 structure, 534 vitamin B 12f: VitaminB coenzyme: 12 oxidation, 376 enzymic role, 534 reduc ion, 376 ethanolamine ammonia-lyase, 575 Wagner-Meerwein rearrangement, glutamate mutase, 549, 571, 575 556 Olefins: Organic solvent soluble corrins, 236 addition to cobalt(I) complexes, Organocobalt complexes: mechanism, 256, 262 synthesis, 245-294 alkylcorrins, photolysis, 302 see also Alkylcobalamins; Alkyl- cobalt(I) complexes, addition, pH cobaloximes; Alkylcorrins; function, 523 Cobaloximes; Cobalt complexes; decomposition, alkylcorrins, 365 Cobalt-carbon bond; Methyl- mechanism: cobalamin; Vitamin B12 coenzyme cobaloximes, addition to, 264 Organolithium reagents, cobalt(III) com- cobalt(I) complexes, addition to, plexes, alkylation, 517 265 OrganometalUc chemistry, vitamin B , hydridocobalt complexes, addition 12 326 to, 265 Ornithine, 328 hydridopentacyanocobalt, addition Orthoamide, vitamin B total synthesis, to, 263 12 178

Outer-sphere electron transfer, Schiff-base P. shermanii, isolation sirohydro- complexes, cobalt(II) complexes, chlorin, 122 519 Palladium(II) al kylcobalt complexes, Oxidation: alkylation, 527 alkylcobalamins, one-electron, 517 Palladium(II) 1 5-cy ano-2,2 ,7,7,12,12- alkylcobaloximes, hexachloroiridate, hexamethyl-1-methylene-AD- table, 515, 516 secocorrin perchlorate, 96 carboxylic acids, corrin, 218 Palladium(II) 1,2 ,2,8,8,12,12-hepta- chromic acid, corrin, 218 methyl-5-cyano-fraHS-corrin cobalt(III) complexes, carbon mono- perchlorate, 95 xide, 515 Paper chromatography, corrin, 249 corrin: Paramagnetic shifts: meso-methyl groups, 239 corrin ring, nmr spectrum, 471

permanganate, 218, 219 nmr spectrum, vitamin B 13r, 487 2,3-dihydroxy-w-propylcobalamin, praseodymium, paramagnetic shift periodate, 284 reagent, 483 dehydrocobinamide, chromic acid, Patterson map, X-ray structure, 97, 98 226 PBG, see Porphobilinogen electrochemical, 517 Pentacarboxylic acid , ele ctronic spe c-

hydrogen peroxide, corrin, 218 trum, vitamin B 12 ,417 methylcobalamin, electrochemical, Pentacyanocobaltate: 517 alkylation, 502 one-electron, alkylcobaloximes, 515 alkyl halides, re activity tow ards, 521

organic radicals, vitamin B12r, 376 1,3-diiodopropane, cyclopropane

vitamin B12: forma ion, 519 chromic acid, 218 olefins from alkyl halides, 519 meso-methyl groups, 239 reaction with: permanganate, 218, 239 acetylene, 276 Oxidation state, alkylcobalt complexes, alkyl halides, table, 274 formal, 514 olefins, 276

Oxidative addition, vitamin B 12 coenzyme recombination with radical inter- enzymic reaction, 576 mediates, 511 Oxidative cleavage: reducing agent, 514 corrin, 217-220 structure, 503 succinimides, corrin, 217 Pentadecaalkylcorrin:

vitamin B12, succinimides, 217 circular dichroism, corrin, 237 Oxime hydrolysis, nitrous acid, vitamin structure, 237

B12 total synthesis, 179 Pentanal, 4,5-dihydroxypentylcobal-

O2, alkylcobalamin photolysis, role of, oxime photolysis, 573 366 3-Pentylcobalamin, rate of, 371

Oxygenated vitamin B 121 ., epr spectrum, Periodate oxidation, 2,3-dihydroxy-rc- 458 propylcobalamin, 284

Oxygen complex structure, vitamin B12r, Peripheral amide (corrin): 459 reactions, 230-234

Oxygen sensitivity, vitamin B 12 coenzyme, vitamin B 12, 230-234

551 vitamin B 12 coenzyme, 41 Ozonolysis: see also Amide groups, corrin periph- corrin, 218 ery heptamethyl cobyrinic acid, 115 Permanganate oxidation: heptamethyl dicyano( 10-bromocobyri- corrin, 218, 239

nate), 218 vitamin B 12, 218, 239 secocorrindione, corrin, 219 Pernicious anemia:

vitamin B 12 , total synthesis, 174, 218 neurological abnormalities, 2

Pernicious anemia (Cont'd) X-ray crystallographic data, vitamin B 12 ,

vitamin B 12, 1 94

P H: X-ray structure, diagram, vitamin B 12, cobalt-free corrin, electronic spectrum, 34

401 see also Vitamin B 12 decomposition rates: Phosphocellulose, corrin chromato- alkylcobinamides, 370 graphy, 249 isopropylcobalamin, 370 5-Phosphoribosyl-l-pyrophosphate, dependence: cobalamins biosynthesis, 153 cobalamins, nmr spectroscopy, 493 Phosphorylation, [R]-l-amino-2- methylcobalamin, nmr spectrum, 494 propanol, 151 descobaltocobamide, electronic spec- Photoaquation: trum, 211 alkylcorrins, 301 function, olefins, cobalt(I) complexes, cobalt-carbon bond, 362 523 cobalt(III) complexes, 296 Phenacylcobalamin, olefin p-complexes, corrin, 330

acid catalysis, 575 Photochemical path, vitamin B12 : Phenolatocobalamin, electronic spectrum, ring closure, 196 404 total synthesis, 169-200 Phenol extraction, corrin, 249 Photochemistry: Phenylacetonitrile, aquocobalamin reac- cobalt-carbon bond: tion with, 279 cleavage, 362 Phenylacetylene, addition to cobalt(I) dissociation energy determination, 507 complexes, 256 secocorrins, metallo, 209 a-Phenylethylamine, resolving agent, vita- a.b, Photoisomerization, methylcorrinoids,

min B 12 total synthesis, 183 301 1 -Phenylethylcobaloximes: Photolability: axial ligands role, activation enthalpy, alkylcobalamins, base-on, off, 303, 524 511 alkylcobalt complexes, 55 3 cob(II)aloximes, reaction with, 504 Photolysis: thermolysis, 304 acetaldehyde:

1-Phenylethyl(pyridine)cobaloxime: ethanolamine and vitamin B 12 coenzyme bond dissociation energy, axial 298

ligands, role, 510 ethylene glycol and vitamin B 12 coen zyme, equilibrium determination, 508 298 cobalt-carbon bond, thermal dis sociation,- alkylcobalamins, quantum yield, 300- 509 303 Phenyl(pyridine)cobaloxime, prepara- alkylcobaloximes, 300-303, 364 tion, Grignard reagent, 271, 278 alkylcobalt complexes, 524, 552 Phenylthiomethyl chloride, reaction anaerobic, alkylcobalt complexes, 553 with corrin, 214 aristeromycyclocobalamin, 297 5'-Phosphate: bis(acetylacetone)ethylenediimine- bond angles, tables, vitamin B 12 , 45- cobalt, alkyl complexes, 524 53 bis(salicylaldehyde)ethylenediimine- bond distances, tables, vitamin B 12, cobalt(III): 45-53 methyl complex, 301 cell dimensions, vitamin B 12 , 94 propyl complex, 302 chemical formula, vitamin B12, 94 bis(salicylaldehyde)ethylenediimine- planarity deviations, vitamin B12, 61 cobalt complexes, alkyl complexes, space group, vitamin B 12 , 94 524 structure, vitamin B12 , 34 carboxylatopentaaminecobalt(III) complexes, torsion around A-D junction, vitamin 272 B 12, 57 carboxymethylcobalamin, 302

Photolysis (Cont'd) 1,4,8,11-tetraazacyclotetradecane, alkyl chloromethylcobalamin, 303 complexes, 524 cobaloximes, 419 trichloromethylcobalamin, 303

cobalt-carbon bond, vitamin Bj 2s, 296 vitamin B 12, 404

5'-deoxyadenosine, vitamin B 12 coenzyme vitamin B 12 coenzyme, 296, 363

and thiols, 299 vitamin B 12r, methylcobalamin, 300

diacetylmonoximeimino diacetylmono- vitamin B 12s: ximatoiminopropane-l,3-cobalt(I), acetone, 302 alkyl complexes, 524 alkylcobalamins, 302 dichloromethylcobalamine, 303 Photoreduction, cobalt(III) complexes, 296 4,5-dihydroxypentylcobaloxime, 534 Pinacoylcobalamin, 371 dihydroxypropylcobalamin: 5,6-dimethylbenzimidazole, 351 glyceraldehyde, 302 pK values: glyceric acid, 302 alkylcobalamins, 494 glycerol, 302 benzimidazole, table, alkylcobalamins, 54,

electronic spectrum, vitamin B12 coen- 351

zyme, 296 benzimidazole, vitamin B12 coenzyme, epr spectroscopy, alkylcobaloximes, 525 351 epr spectrum, nitroalkylcorrins, 405 bis(acetylacetone)ethylenediiminecobalt, ethane, methylcobalamin, 300 504 ethylcobalamin, 302 bis(salicylaldehyde-o-phenylenediimine)

frozen solution, epr, vitamin B12 coen- cobalt, 504

zyme, 299 7,7'(CH3 )2 bis(salicylaldehyde)ethylene- 3-hydroxyisopropyl(pyridine) cobaloxime, diiminecobalt, 504 302 carboxymethylcobalamin, 316 2' ,3' ,0-isopropylidene-5 '-deoxy uridyl- cobalt, hydrides, 335 cobalamin, 297 corrin, raeso-methyl groups, 239 methylcobalamin, 300, 362, 404 diacetylmonoximeimino diacetylmono- methylcobaloxime, cob(II)aloximes, 301 ximatoiminopropane-1,3-cobalt, methylperoxocobaloxime, methylcobalo- 504 xime, 553 hydridocobalamin, 506 methyl radicals, methylcobalamin, 300 hydridopentacyanocobalt, 506 model for eth anolamine ammonia ly ase, hydrido(tri-H-butylphosphine) cobalo-

vitamin B 12 coenzyme, 298 xime, 506 nitroalkylcobalamin, 405 steric effects, neocobalamins, 489 nitroalkylcobinamide, 405 vitamin B 12 coenzyme, model systems, olefins, alkylcorrins, 302 504 pentanal, 4,5-dihydroxypentylcobalo- vitamin B 12 , meso-me hyl groups, 234 xime, 573 vitamin B 128 , 364 in presence of nitrosodurene, vitamin Planarity:

B 12 coenzyme, 298 cobaloximes, 505

in presen ce of thiols, v itamin B 12 coen- cobalt corrins, 54, 61, 208 zyme, 298 Platinum(IV) alkylcobalt complexes, propylcobalamin, 302 alkylation, 527 propylcobaloxime, 302 Pleochroism, vitamin B 12 crystal morpho logy, quantum yield: 25 alkylcobaloximes, 525 Polarizability, nmr spectroscopy cobalt- alkylcobalt complexes, 55 3 c arbon bond,489

vitamin B 12 coenzyme, 303 Polarization effects: radical traps, alkylcobalt complexes, corrin, electronic spectrum, 402 vitamin B , 402 553 12 Porphobilinogen, incorporation into corrin, role of O 2, alkylcobalamins, 366 111 spin-traps, alkylcobalt complexes, 553

Porphobilinogen deaminase: hydridocobalamin, secondary alkyl- corrin biosynthesis, 139 corrinoids, 253,365,552 deamination, aminomethylbilanes, 118 hydrido(tri-w-butylphosphine)cobalo- 13 [8- C] Porphobilinogen, vitamin B 12 bio- xime, 253 synthesis, 480 b-hydroxy-n-propyl(pyridine)coboloxime, Potassium reduction, cobalt complexes, 254 257 Powder samples, vitamin B12r epr spectro- 4-hydroxy-2,2,6,6-tetramethylpiperidine- scopy, 439 N-oxylcobamide coenzyme, 267 Praseodymium corrin shift reagent, table, lactones (corrin ring), 226 483 methyl(aquo)cobyrinic hepta tert- Preferred coordination number, cobalt com- alcohol, 278 plexes, 504 l-methyl-2,2-diphenylcyclopropyl Preparation: (pyridine)cobaloxime, 254 acetoxyalkylcobaloximes, 284 N-methyleneaniline(pyridine)cobalo- 1-adamantyl(pyridine)cobaloxime, 255 xime, 258 8-aminocobyrinic acid abcdefg-hexamethyl 10-nitrosocobalamin, 217 ester c-lactam, 236 l-norbornyl(pyridine)cobaloxime, 255 8-aminoethylcobalt complexes, 2§7 phenyl(pyridine)cobaloxime, 271 benzoyl(l-pyridino)methanide(chloro) pulse radiolysis, a-hydroxyalkylcobalt cobaloxime, 276 complexes, 273 10-bromocobalamin, 216 reactions, 2-hydroxyalkylcobaloximes, b-carbomethoxyphenylcobinamide, 271 284 15-carboxy-15-norcobinamide, 239 rhodium cobyrinic acid-c,c-diamide, 37 10-chlorodehydrovitamin B12, 215 sirohydrochlorin, 257 Coa-cyano-Cob-alkylcobamides, 307 p-trifluoromethylphenyl(pyridne) cobalo- cobalt(III) complexes, cobalt-carbon xine, 271 bond, 271-277 vinylcobaloxime, 261 cobyrininic acid-tf,c-diamide, 37 vinylcobalt porphyrins, diazoalkanes, 280 corrin, organic solvent soluble, 236 vitamin B 12 coenzyme analogs, 5'-deoxy- cyclohexyl-3,5,6-trimethylbenzimi- 5'-halonucleosides, 267 dazoylcobamide, 255 vitamin B 12: dansylamidopropylcobalamin, 267 carboxylic acids, 231 6 5 '-deoxy( 1 ,N -etheno)-adenosylco- yellow corrinoids, 215, 228-230 balamin, 285 vitamin B 12r, 439 2,6-diaminonebutavinylcobalamin, 267 yellow corrinoids, gCoPSE, 40 5,15-dicarboxy-5,15-dinorcobinamide, Preuro'gen, 118

239 Principal axes, vitamin B 12r epr dicobaloximes, 268 spectroscopy, 439 2.2- diethoxyethylcobalamin, 28 1 Prokaryotes: dihydroxyalkylcobaloximes, 284 cobalt-carbon bond biosynthesis, 1.2- dioxa-2-cyclopentylmethylcobalo- 155- 163

xime, 282 vitamin B 12 coenzyme biosynthesis, 6 l,N -ethenoadenosylcobalamin, 267 156- 161 formycinylcobalamin, 267 Propane-1,2- diol , see Propylene gly col 2 formylmethylcobalamin, 283, 315 [I- H2 ]Propane-l,2-diol, vitamin B 12 formylmethylcobaloxime, 315 coenzyme kinetic isotope effect, Grignard reagent, phenyl(pyridine)cobalo- 554 xime, 278 Propanolamine, v itamin B 12 coenzy me halomethylcobalt porphyrins, diazo- nmr spectrum, 465, 470 methane, 280 Propargyl alcoho l, addition to cobalt(I) heptamethyl dicyano-5, 15-bisnorco- complexes, 256 byrinate, 239 Propionaldehyde, 328 heptametyl dicyanocobyrinate, 236 Propionamide side chain, vitamin B12 , 30

Propionibacterium arabinosum, nucleotide Protoporphyrin IX, structure, 110 loop biosynthesis, 152 Prototrophs, cobalamins, 155 Propionibacterium shermanii: Puckering, corrin ring, 54 corrin, biosynthesis, 112 Pulse radiolysis: source of corrin, 146 acetaldehyde, ethylene glycol, 574 Proposed mechanisms, isomerase aquocobalamin, 318 reactions, 383 Me[14] -diene N4, 574 Propylaquocobaloxime, redox poten- 1,2-dihydroxyethyl radical, 574 tial, 516 a-hydroxyalkylcobalt complexes, Propylbis(acetylacetone)ethylenediimine- preparation, 273

cobalt, radical scav engers, therm al vitamin B 12, 318

decomposition, 512 vitamin B 12 coenzyme, 318

Propyibis(salicylaldehyde)ethy Iene- vitamin B 12r-, 318 diiminecobalt, radical scavengers, Purification, methyltransferase enzyme, thermal decomposition, 512 135

Propylbis(Salicylaldehyde)-O -phenylene- Purine nuleosides, vtamin B12 coenyme, diiminecobalt, ra dical scavengers, 300 thermal decomposition, 512 Pyrazolopyrimidine nucleosidylcobalamin, Propylcobalamin, photolysis, 302 reac ion with cyanide, 307 Propylcobaloxime, photolysis, 302 Pyridinatocobalamin, electronic spectrum, n - Propylcyanocobalamin, electronic 411 spectrum, 413 Pyridine complexes, hydrolysis, alkyl- Propylene glycol, 328 cobalaoximes, 248 Propyl(pyridine)bis(salicylaldehyde-o- Pyridoxal phosphate: phenylenediimine)cobalt, bond aminomutases, 329 dissociation energy, 512 cofactor, 2,6-diaminohexanoate Propyne, addition to cobalt(I) com- mutase, 574 plexes, 256 Pyrolysis: Prosthetic group sulfite reductase, cobalt-carbon bond, 303 siroheme, 128 vitamin B12, 239 Protection by peripheral groups, 14 cobalt-carbon bond, 90 N-Quadrupole interaction, vitamin B 12r,

Protection by side chains, vitamin Bu 441 coenzyme cobalt-carbon bond, 41 Quantum yield: Protein: alkylcobaloximes, photolysis, 524 cobalt-carbon bond, labilization, 333 alkylcobalt complexes, photolysis, 553

distortion, vitamin B12 coenzyme, photolysis, alkylcobalamins, 303 373 vitamin B 12 coenzyme, photolysis,

vitamin B 12 coenzyme: 303 enzymic reaction, 555 role of, 329 Racemization, X-ray crystallography, Protein effects, cobalt-carbon bond R-a-cyanoethyl(S-a-methyl- angles, 373 benzylamine)cobaloxime, 88 Protonated: Radical cations, vitamin B 12 coenzyme,

nmr spectrum, vitamin B 12 coenzyme, ethanolamine ammonia-lyase, 466 573 radical intermediates, 557 Radical doublet intermediates: Protonation: enzymic reaction epr spectroscopy, alkylcobalamins, 351 450 nmr spectroscopy, 5,6-dimethyl- vitamin B12 coenzyme enzymic benzimidazole, 494 reaction, 450

vitamin B 12 coenzyme, 351 Radical intermediates:

vitamin B 12s, 364 aminomutases, 556

Radical intermediates (Cont'd) methylcobalamin, 368 bis(salicylaldehyde-o-phenylene- neopentylcobalamin, 368 diimine)cobalt(II), alkyla- 2- norbornylcobalamin, 368 tion, 518 2- methyl-2-butylcobalamin, 371 cobalt(II) complexes, alkylation, organic radical recombination, vitamin

518 B 12r -, 525 diol dehydrase, 556 3- pentylcobalamin, 371 enzymic reaction, 2-amino-l-propanol, pinacoylcobalamin, 371 450 Rates, alkylcobaloxime axial ligand ethanolamine ammonia-lyase, 556 exchange, 248 glutamate mutase, 556 Rates of hydrolysis, steric, amide groups hydrido(tri-n-butylphosphine)- (corrin periphery), 231

cobaloxime, olefin addition, Ratio, methylcobalamin, vitamin B12 518 coenzyme, 161 a-methyleneglutarate mutase, 557 Reaction pathways: pentacyanocobaltate, recombination diol dehydrase, 555, 558 with, 511 ethanolamine ammonia-lyase, 555 protonated, 557 olefin p-complexes: vitamin B 12r alkylation, 520 aminomutases, 573 Radical pair recombination, CIDNP diol dehydrase, 575

measurements, 512 vitamin B12 coenzyme: Radical reactions, vitamin B12, yellow enzymic reaction, 555 corrinoids, 229 ethanolamine ammonia-lyase, 573 Radical rearrangements: glutamate mutase, 571 aminoalcohols (vicinal), 573 a-methyleneglutarate mutase, 570 1,2-diols, 573 methylmalonyl-CoA mutase, 565, 566 Radical recombination: Reactions: corrin, 363 alkyl ugands, 295-323 vitamin Blsr, 363 cobalt(I) complexes, 263 Radical scavengers, alkylcobalt com- 5 '-deoxyadenosyl radical, formation, 297, plexes, 301, 512 363 Radical transfer, cobalt-carbon bond 2-hydroxyalkylcobaloximes, preparation, cleavage, 526 284 Radical traps, alkylcobalt complexes, methyl radicals, 300 photolysis, 553 nucleotide loop, 234-236 Rapid reaction intermediate: peripheral amide groups (corrin), 230-234

epr spectrum: vitamin B12, chloramine T, 215 epr spectroscopy, 455 Reaction with: ribonucleotide reductase, 455 acetylene, pentacyanocobaltate, 276 ethanolamine ammonia-lyase, 455 acid: vitamin B12 coenzyme, enzymic alkylcobalamins, 313 reaction, 455 l,3-dioxo-2-cyclopentylmethylcobala- Rate of: min, 315 acid catalyzed decomposition: formylmethylcobalamin, 314 2-butylcobalamin, 371 hydroxyalkylcobaloximes, 313 isopropylcobalamin, 371 4-hydroxy-n-butylcobaloxime, 314 decomposition: 3- hydroxy-n-propylcobaloxime, 314 alkylcobalamins, very strained, 365, (3-hydroxy-H -propylpyridinato- 368, table, 371 cobaloxime, 314 cyclobutylcobalamin, 368 methyl(aquo)cobaloxime, 313 cyclohexylcobalamin, 368 vinylcobalamin, 314 cyclopentylcobalamin, 368 alkali: cyclopropylcobalamin, 368 adenosylcobaloxime, 307

Reaction with (Cont'd) alkylcobalamins, 306 cob(I)aloxime, 2-hydroxycthylco- aristeromycyclocobalamin, 306 baloxime, 310 N-benzoyladenosylcobalamin, 306 cyanocthylcobalamin, 310 Coa-adenyl-Co(3-adenosylcobalamin, dihalomethylcobaloximes, 309 305 halomethylcobaloximes, 308 Coa-aquo-Co(Jadenosylcobamide, 306 (3-hydroxyalkylcobaloximcs, 310 Coa-aquo-Co(3-adenosyl(3,5,6-trimethyl- trans-2-hydroxy cyclohexy lcobaloxime, benzimidazolecobamide), 306 311 difluorochloromethylcobalamin, 307 hydroxycthylcobalamin, 311 formycyclobalamin, 307 hydroxyethylcobinamide, 311 pyrazolopyrimidine nueleosidylcobala- me hoxycarbonylethylcobalamin, 310 min, 307 trimethylaminoethylcobalamin, 310 N-tosylcytidylcobalamin, 306

vitamin B 12 coenzyme, 307 triethylaminoethylcobalamin, 307 alkyl halides, cobalt(II) complexes, 273 trifluoromethylcobalamin, 307

alkyl halides, table: vitamin B 12 coenzyme, 305

pentacyanocobaltate, 274 a,b-dibromoe hyl acetate, vitamin B 12

vitamin B 12r, 274 coenzyme, 285 aquohydroxo Co(III): electrophiles, cobalt-carbon bond, 312-317 acetone, 336 equilibrium data, cob(II)aloximes, 504

nitromcthane, 336 hydrogen cyanide, vitamin B12 coenzyme,

aiyl halides, vitamin B 12 s , 271 306

ascorbic acid, vitamin B 12, 229 hydroxide: carbanions: aristeromycylcobalamin, 307 bissalicylaldehyde)ethylenediimine- cob(I)aloxime, trifluoromethyl- eobalt(III), 279 cobaloxime, 309 cobalt(III) complexes, 279 b-hydroxyisopropylcobaloxime, 310 cob(I)aloxime, 1,1 ,bis-(p-chlorophenyl)- b-hydroxy-n-propylcobaloxime, 310 2,2,2-tiichloioethane, 266 hydroxylamine: cobalt(I) complexes: acetylcobalamin, 312

threo-3,3-dimethylbutyl-l ,2-d2 -tri- acetylglycobalamin, 312 fluoromethyl sulfonate, 260 glyglycobalamin, 312

epoxides, 256 iodine, vitamin B12 , 226 etheneimine, 257 kinetics: cobalt(III) complexes: cob(II)aloximes, 504 carbenes, 279 cobalt(II) complexes, 273 enols, 279 table, cobalt(II) complexes, 274 ethyl vinyl ether, 281 malononitrile, aquocobalamin, 279 2-hydroxyethyl vinyl ether, 282 mercaptides: malononitrile, 279 alkylcobaloximes, 311 cobinamide guanosine diphosphate, methyl(aquo)cobaloxime, 311 5,6-dimethylbenzimidazole-5- metal ions, cobalamins, 495 nucleotide, 153 methylmagnesium iodide, heptamethyl- corrin: cobyrinate, 278 chloramine T, 215 methylmercaptide, methylcobalamin, 311 dimethyl(methylene)ammonium iodide, olefins, pentacyanocobaltate, 276 213 organic radicals, cobalt(II) complexes, hydratcd electrons, 318 271 nitrosyl chloride, 217 phenylacetonitrile, aquocobalamin, 279 phenylthiomethyl chloride, 214 1 -phenylethylcobaloximes, cob(Il)alo- cyanide: ximes, 504 ara-adenosylcobalamin, 306 styrene and hydrogen, cob(II)aloximes, L-adenosylcobalamin, 306 504

Reaction with (Cont'd) vitamin B 12r methyl radicals, 553 tetracy anoethylene: Redox chemistry: alkylcobalt complexes, 285 alkylcobaloximes, 515 cinnamyl(imidazole)cobaloxime, 286 cobalt, unique biologically, 340

trifluoroacetic acid, vitamin B 12 , 223 diacetylmonoximeimino diacetyl- vinyl ethers, cobalt(III) complexes, 281 monoximatoiminopropane-1,3-

vitamin B 12 coenzyme, nitrosodurene, cobalt, alkyl complexes, 514 298 model systems:

vitamin Bnr: vitamin B 12,513 benzyl bromide, 513 vitamin B 12 coenzyme, 513 5 '-deoxyadenosyl radical, 373 Schiff-base complexes, Cobalt com-

vitamin B12s : plexes, 514

benzyl bromide, 513 vitamin B 12 coe nzyme, model sy stems,504 cyclodecyl-l-d-iodide, 261 Redox potential: dimethylbromome hyl)malonate, 564 alkylcobaloximes, table, 516 Reactivity toward: aquocobalamin, 514 alkyl halides, table cobalt(II) complexes, benzylaquocobaloxime, 516 521 bis (acetylacetone)ethy lenediimine- bis (salicylaldehyde-o -phenylenediimine)- cobalt, bis(salicylaldehyde)- cobalt(II)(py), alkyl halides, 521 ethylenediiminecobalt, 504 pentacyanocobaltate, alkyl halides, 521 bis (salicylaldehyde-o-phenylenediimine)- triphenylphosphine cob(II)aloximes, cobalt, 504 alkyl halides, 521 cobalt(I) complexes, electron-donor vitamin B 12r, alkyl halides, 521 strength, ligand, 251, 504 Rearrangements: diacetylmonoximeimino diacetyl- but-3-enylcobalamin, cyclopropyl- monoximatoiminopropane-1,3- carbinylcobalamin, 567 cobalt, 504 but-3-enyl(pyridine)cobaloxime, cyclo- isopropylaquocobaloxime, 516 propylcarbinyl(pyridine)- methyl(aquo)cobaloxime, 516 cobaloxime, 568 propylaquocobaloxime, 516

but-3-enyl radical, cyclopropylcarbinyl vitamin B 12 coenzyme, model systems, radical, 557 504 cyclopropylcarbinylcobalamin, 379 Reduced forms, sirohydrochlorin, 123 cyclopropylcarbinylcobaloximes, 381 Reduction: cyclopropylcarbinyl radical, 557 acetic acid, carbon dioxide, 528 1,2-dihydroxyethyl radical, 532 aquocobalamin, enzymic, 157 kinetics, cyclopropylcarbinyl radical, chromium(II), cobalt complexes, 254 567 cobalt complexes: 1-methyl-6«r-3-enyl(pyridinc)cobaloxime, hydrogen,252 3-methyleyclopropy lcarbinyl- potassium, 254 (pyridine)cobaloxime, 569 sodium, 254 2-methyl-6ur-3-enyl(pyridine)cobaloxime, sodium amalgam, 254 1-methyl-tor -3-cnyl(pyridine)- sodium borohydride, 251 cobaloxime, 569 diaquocobinamide, formate, 447 organic radicals, 531, 556 electrochemistry, cobalt complexes, 254 role of cobalt, organic radicals, 533 FAD, cobalamins, 157 Recombination: FMN, cobalamins, 157

alkyl radicals, cobalt, 335 LiAlH4 , heptamethyl dicyanocobyrinate CIDNP measurements, radical pairs, 512 237 cob(II)alamin, methyl radicals, 511 mcthylcobalamin, carbon dioxide, 528 Cobalt(II) complexes, methyl radicals, 335 NADH, cobalamins, 157 radical intermediates, pentacyanocobaltate, nickel 1,19-dimethyloctadehydrocorrin, 511 catalytic, 238

Reduction (Cont'd) comparison to, cobalt complexes, 72

organic radicals, vitamin Bnr, 376 folding, 60 sirohydrochlorin, sirolactone, 122 planarity deviations, 61 sodium borohydride: structure, 34 cobaloximes, 251 torsion around A-D junc ion, 57 cobalt complexes, 251 X-ray crystallographic data, 72 thiols, cobalt complexes, 254 Rhodium dicyano[cobyrinic acid-a-c-

zinc/acetic acid, vitamin B12a, 365 diamide]:

Reduction of vitamin B12 , ribonucleotide cell dimensions, 94

reductase, vitamin B 12r, 434 chemical formula, 94 Reduction to heptaol, heptamethyl dicyano- space group, 94 cobyrinate, 226 X-ray diffraction data, 94

Reductive alkylation: b-Ribazole, vitamin B 12 total synthesis, cobaloximes, 248 198 cobalt complexes, mechanism, 250, 258- Ribonucleotide reductase: 267 affinity chromatography, 268

Reductive arylation, electron transfer, 5'-deoxyadenosine, vitamin B 12 mechanism, 3 cobalt complexes, coenzyme, 577

271 5-deoxyadenosyl radical, vitamin B, 2 Reductive cleavage: coenzyme, 577

alkylcobalamins, vitamin B121 ., 317 epr spectroscopy, enzymic reaction, carbon monoxide, cobalt-carbon bond, 558 515 epr spectrum, enzymic reaction, 451 cobalt-carbon bond, 317 from Escherichia coli, 545

methylcobalamin, H2 /Pt, 317 hydrogen exchange, with solvent, 449 thiols, cobalt-carbon bond, 515 rapid reaction intermediate, epr spectrum,

Refractive index, vitamin B 12 crystal mor- 455

phology, 25 thiyl radical, vitamin B 12 coenzyme, 577

Regiospecific aldol, vitamin B 12 total vitamin B 12 coenzyme, enzymic reaction, synthesis, 179 529

Resonance Raman spectrum, corrin, 398 vitamin B 12r formation, Lactobacillus

Retro-Claisen, vitamin B 12 total synthesis, leichmanni, 439 174 vitamin B12r: Reversibility: binding to, 442

b-elimination, 367 reduction of vitamin B12,434

vitamin B 12 coenzyme, enzymic reaction, D-Ribose, vitamin B12 total synthesis, 198 544 Ribose-l-phosphate, cobalamins biosyn thesis, R factor, X-ray structure, 97 153 R+ from (alkylcobalt)+, crystallography, Ribose ring:

R-a -cyanoethyl(S-a -methylbenzyl- conformation, vitamin B 12 coenzyme, 550 amine)cobaloxime, 88 554 Rhodium: nmr spectrum(13 C), 478

incorpora ion into: vitamin B 12 coenzyme, nmr spectrum, 465, 15-cyano-l,2,7,7,12,12-hyptamethyl- 470

corrin, 211 Ring C, vitamin B 12 total synthesis, (+) camphor,

vitamin B12, 211 184

Rhodium analog, vitamin B12,211 Ring closure, 190, 196 Rhodium cobyrinic acid-a,c-diamide: photochemical, secocorrins, 196

preparation, 37 vitamin B12, total synthesis, 197

X-ray structure, diagram, 34 Ring puckering, vitamin B 12 coenzyme, Rhodium corrin: 41

bond angles, tables, 45-53 Rings A -D, vitamin B 12 total synthesis, 197

bond distances, tables, 45-53 Rings B-C1 vitamin B 12 total synthesis, 197

Ring structure, yellow corrinoids, 37 Selenocyanocobalamin, 93 Role in formation of yellow corrinoids, Sephadex corrin chromatography, 249 ascorbic acid, 39 Shift reagent, corrin ring, gadolinium(III),

Role in vitamin B12 chemistry, cobalt, 333, 472,482 335 Side chain:

Role of: amide, vitamin B12 , hydrolysis, 33 cobalt, organic radicals, rearrangements, conformations: 533 corrin, 208 cobalt-carbon intermediate, carbon- corrin ring, 52, 54, 63 skeleton rearrangements, 382 table, 52, 54 4s and 4p orbitals, cobalt-carbon bond, vitamin B12, 208 338 corrin, 63 13 model systems, vitamin B 12 coenzyme, corrin ring, nmr spectrum( C), 480 mechanism, 528 disorder, vitamin B 12 monocarboxylic

O 2 , alkylcobalamin photolysis, 366 acid (E2) X-ray structure, diagram,

protein, vitamin B 12 coenzyme, 329 34 modification, binding to apoenzyme, 65

7,7'(CH3 ) 2 SALEN, structure, 503 vitamin B 12 :

Scavenger, vitamin B 12r, methyl radicals, acetamide, 30 300 propionamide, 30

Schiff-basc complexes: vitamin B12 coenzyme, cobalt-carbon acidity, 506 bond, protection, 41 alkylcobalt complexes, bond dissociation Sign inversion, circular dichroism, corrin, energy, 512 422 alkylcobalt(IV) complexes, 516 Simulation: cobalt complexes, redox chemistry, 514 azidocob(II)inamide, epr spectrum, 445 cobalt(lll) complexes, outer sphere cob(II)amides, epr spectrum, 446 electron transfer, 519 histidine cob(II)amide, epr spectrum, Secocorrindione: 445

corrin ozonolysis, 219 Single crystals, vitamin B 12r epr spec troscopy, cyclization, corrin, 220 439 structure, 219 Siroheme: Secocorrins: demetallation, 128 bond angles, distances, tables, 45-53 prosthetic group, sulfite reductase, Intermediates in corrin biosynthesis, 128 116 Sirohydrochlorin: metal complexes, X-ray diffraction data, biosynthesis, 126 96 bislactone, 122 metallo, photochemistry, 209 circular dichroism, 122 ring closure, photochemical, 196 conversion to, sirolactone, 126 structure, 78, 116 incorporation into: torsion around A-D junction, 57 C tetanomorphum, 126 total synthesis, 196 cobyrinic acid, 126 X-ray crystallographic data, metal interconversion, sirolactone, 123 complexes, 77 isolation, desulfoviridin, 122 Secondary alkylcobalamins, 255 monolactone, 122 Secondary alkylcorrinoids, preparation, octamethyl ester: hydridocobalamin, 552 electronic spectrum, 125 Sclenocyanatocobalamin, electronic nmr spectrum, nuclear Overhauser spectrum, 411 effect, 130 Selenocyanide: P. shermanii, isolation, 122 selenium location, vitamin B 12, 27 preparation, 257 X-ray diffraction data, vitamin B12, 26 reduced forms, 135

Sirohydrochlorin (Cont'd) Spiro lactones (corrin ring), 226 sirolactone reduction, 122 Stability: structure, 122-124 benzylcobalamin, 255 Sirolactone: benzylcobalt(octaethylporphyrin), from P. shermanii, 123 255 heptamethyl ester, nmr spectrum, cobalt, hydrides, 335 125 cobalt-carbon bond, vitamin B12 octamethyl ester, 122 coenzyme, 330, 335, 366 reduction, sirohydrochlorin, 122 Stabilization: sirohydrochlorin: 5-deoxyadenosyl carbocation, 549 conversion to, 123 5'-deoxyadenosyl radical, 548 interconversion, 123 Stable 5-coordinate cobalt(III) com- structure, 123, 124 plexes, 506 see also Corriphyrin-4, structure Stable yellow corrinoids, see Yellow Sodium amalgam reduction, cobalt corrinoids complexes, 254 Standard electronic spectrum, vitamin Sodium borohydride: B12 , conversion to dicyano- cobaloximes, reduction, 251 cobalamin, 395 cobalt complexes: Stereochemistry: catalysis, 252 alkylcobalt complexes, mercury(II), reduction, 251 526 reduction, cobalt complexes, 251 alkynes, addition to, 256 Sodium reduction, cobalt complexes, cob(I)aloximes, alkylation, 523 254 cobalt-carbon bond, halogen Solu ion thermolysis, ethylcobalamin, cleavage, 316 304 cobalt(I) complexes, alkylation, Solvent effects: 523 electronic spectrum: methionine, methylation, 113

vitamin B12 , 409, 410 (S)-methylheptylpyridinatocobal-

vitamin B12 coenzyme, 410 oxime, iodine cleavage, 317 Space groups, corrin derivatives, 93- vinyl halides, alkylation, cobalt(I) 97 complexes, 260 Spectrochemical series, rnzns-effect, vitamin B 12s, alkylation, 260, 523 336 Stereospecific thermal cyclization, Spin-forbidden transitions, electronic vitamin B 12 total syn hesis, spectrum, 406 176 Spin-Hamiltonian: Steric compression: cobalt(II) complexes, 436 distortion cobalt-carbon bond, 359

vitamin B 12 r , 441 X-ray structure, vitamin B 12 co-

Spin-labelled analogs, vitamin B 12 enzyme, 359 coenzyme, 267 Steric crowding: Spin-lattice relaxation times: bond length, cobalt-carbon bond, carboxymethylcobalamin, 492 505 ethylcobalamin, 492 cobalt-carbon bond strengths, 506 hydroxyethylcobalamin, 492 vitamin B 12,506 methylcobalamin, 492 vitamin B12 coenzyme, 506

vitamin B12 coenzyme, 492 Steric distortion, effects, 367 Spin-trapped nitroxides, 2 98 Steric effects: Spin-traps, alkylcobalt complex bond dissociation energy, cobalt- photolysis, 553 carbon bond,512 Spirocyclic intermediate: cobaloximes, 86 corrin biosynthesis, 118 cobalt-carbon bond, bond dis- structure, 119 sociation energy, 531

Steric effcets (Cont'd) cobalt 2,2,7,7,12,12-hexamethyl- cobalt-carbon bond angles, 355, corrin, 424 372 cobalt 7,7,12,12-tetramethyl-

ligand equilibria, vitamin B 12 co- corrin, 424 enzyme, 341 cobinamides, 235 ligand exchange, alkylcobalamins, cobyric acid, 34, 148, 170 341 cobyrinic acid, 109 neocobalamins, pK values, 489 corriphyrin-3, 134 origin, corrin, 355 corriphyrin-4, 124 on structure, alkylcobalamins, 341 corrole, 203 transmission, corrin, 355 15-cyano-l,2,2,7,7,12,12-hepta- Steric interactions: methylcorrin, 211 cobalt-carbon bond, labilization cyclic nucleoside, 554

by, 361 dehydrovitamin B 12, 215 with corrin ring, epr spectrum, 5'-deoxy-8,5'-cycloadenosine, 297 5,6-dimethylbenzimida zole, diacetylmonoximeimino diacetyl- 448 monoximaloiminopropane- epr spectrum: 1,3-cobalt, 503 cobinamides, 448 dicyanocobyric acid, 206

vitamin B12r, 442, 448 4 ',5 -didehy dro-5 '-deoxyaristeromy cin, Steric requirements, corrin, axial 297 ligands, 255 dimethylated isobacteriochlorins, Strain orbital: 123-126 corrin, 400, 411 8-epicobalamin, 225

vitamin B 12 coenzyme, 411, 560 13-epicobalamin, 224 Streptomyces griseus, methylcobala- 3-episirohydrochlorin, 129 min biosynthesis, 161 Factor I, 130, 131

Structural comparison to vitamin B 12, heptamethylcobyrinate, iodide

vitamin B12 coenzyme, 41 complex, 72 Structural information, nmr spectro scopy,- heptamethyl cobyrinic acid, 114 482 5,7,7,12,14,14-hexamethyl-1,4,8,11 - Structure: tetraazacyclotetradeca-4,11- adenosine-5'-carboxaldehyde, 297 dienecobalt, 574 aminomethylbilane, 118 iodocobalt(II) cobyrinic acid hepta- aquocyanocobyric acid, 205 methyl ester, X-ray crystal- bis(acetylacetone)ethylenediimine- lographic data, 69 cobalt(IIl), 503 2',3',0-isopropy lidenecyclodihydro- bis(salicylaldehyde)ethylenediimine- uridine, 298 cobalt, 557 Me[14]-diene N4, 574 bis(salicylaldehyde)ethylenediimine- methyl(aquo)cobyrinic hepta cobalt(III), 503,552 ferf-alcohol, 278 bis(salicylaldehyde-o-phenylene- mono-C-methylated chlorin, 131 diiminecobalt(III), 503 neovitamin B 12, 34, 224 bridged cobaloximes, 87, 269 2,2,7,7,12,13,17,18-octamethyl- capped cobaloximes, 533, 565 isobacteriochlorin, 136 cobalocorrin, 203 olefin p-complexes, 534 cobaloxime, 246 pentacyanocobaltate, 503 cobalt 15-cyano-2,2,7,7,12,12- pentadecaalkylcorrin, 237 hexamethylcorrin, 424 protoporphyrin IX, 110 cobalt 15-cyano-7,7,12,12-tetra- rhodium corrin, 34 methylcorrin, 424 7,7'(CH3 ) 2 SALEN, 503 cobalt 2,2,7,7,12,12,15-hepta- secocorrindione, 219 methylcorrin, 424 secocorrins, 78, 116

Structure (Cont'd) isobacteriochlorins, 135 sirohydrochlorin, 122-124 2,2,7,7,12,13,17,18-octamethyliso- sirolactone, 124 bacteriochlorin, 136 spirocyclic intermediate, 119 organocobalt complexes, 245-294 1,4,8,11-tetraazacyclotetradecane, work up of reaction mixtures, cobalt- 503,552 carbon bond formation, 248 trimethylated isobacteriochlorins, 132,134 Synthetic analogs, vitamin B 12 coenzyme, uroporphyrin I, 118 332 uroporphyrin III, 110 Synthetic utility, vitamin B12r alkylation, uroporphyrinogen III, 110 277

vitamin B 12: hexacarboxylic acid, 28, 204 Temperature dependence, cobalamin nmr c-lactone, 227 spectroscopy, 490 monocarboxylic acid, 34 Temperature variation, corrin electronic 5-phosphate, 24, 34, 170 spectra, 348, 407

vitamin B 12 coenzyme, 19, 25 Template reactions, vitamin B12 total

vitamin B 12r, oxygen complex, 459 synthesis, 188 yellow corrinoids, gCoPSE, 37-40, 42, Tertiary alkyl, cobaloximes, 254 228-230 1,4,8,11-Tetraazacyclotetradecane- zinc 15-cyano-2,2,7,7,12,12-hexa- cobalt(III): methylcorrin, 424 alkyl complexes, photolysis, 271, 524 see also X-ray structure cobalt-carbon bond, energy, 554 a-Styrylcobaloxime, thermolysis, 304 cobalt(II) reaction with alkyl halides, b-Substituted alkylcobalamins and alkali, 274

vitamin B 12s , 310 model, vitamin B12 coenzyme, 551

meso-Substitution, vitamin B 12 , 212 structure, 503, 552 Substrate radicals: vitamin B 12 coenzyme model systems,

vitamin B12 coenzyme-mediated re action, 551 382 Tetracarboxylic acid: vitamin B 12r -, intermediate, interaction circular dichroism, 421 with, 382 electronic spectrum, 415 Succinimides: Tetracyanoethylene: corrin, oxidative cleavage, 217 alkylcobalt complexes, reaction with,

oxidative cleavage, vitamin B12, 217 285 Succinyl-CoA, 328 cinnamyl(imidazole)cobaloxime, re- Sulfite and nitrite reductases, isobacterio- action with, 286

chlorins, 122 Tetracyclic lactam, vitamin B 12 total Sulfite reductase, siroheme prosthetic synthesis, 174 group, 128 Tetradehydrocorrin, nomenclature, 19 Sulfitocobalamin, electronic spectrum, 347, Tetrahydrochlorins, see Dihydroiso- 411 bacteriochlorins, Factor I Sulfomethylcyanocobalamin, electronic Tetrahydrofolic acid, 528 spectrum, 413 Tetrakis-(didehydro)corrin, nomenclature, Sulfonatocobalamin: 19 halogenation, 216 Thallium(III): lactam formation, 226 alkylation, alkylcobalt complexes, 526

Sulfur extrusion reactions, vitamin B12 cobalt-carbon bond cleavage, 526 total synthesis, 185, 190 Theoretical considerations, electronic Synthesis: spectrum, 396 alkynylcobalt complexes, 279 Theoretical studies: 1-amino-2-propanol, 13 bridged cation, 557

analysis of reaction mixtures, cobalt- vitamin B 12 coenzyme, enzymic reaction, carbon bond,247 557

Theory: cobalt complexes, reduction, 254 epr spectroscopy, 435 methylcobalamin methyl transfer, 312 vitamin B12 coenzyme, mechanism of photolysis, 5-deoxyadenosine, vitamin

action, 543-582 B12 coenzyme, 299 Thermal cleavage, cobalt-carbon bond, Thioredoxin, 545

362 Thiyl radical, vitamin B 12 coenzyme ribo- Thermal decomposition, alkylcorrins and nucleotide reductase, 577 radical scavenging, 512 L-Threonine, conversion to D-l-amino-2- Thermal dissociation, 1-pheny lethyl- propanol, 199 (pyridine)cobaloxime, cobalt- Threonine decarboxylation, [R]-l-amino- carbon bond,509 2-propanol, 150 Thermal stability, benzylcobalt complexes, Timing, cobalt-carbon bond biosynthesis, 513 155-163 Thermochemical, cobalt-carbon bond dis- Tin(IV), alkylcobalt complexes, alkylation, sociation energy determination, 527 507 Torsion around A-D junction, corrin Thermodynamics, ligand exchange, table, derivatives, 57 5,6-dimethylbenzimidazole, 496 Torsion angles, C(l)-C(19) bond, 56 Thermodynamic stability, cobalt-carbon N-Tosylcytidylcobalamin, reaction wi h bond,336 cyanide, 306 Thermolysis: Total synthesis of vitamin B12: alkylcobalamins, cobalt-carbon bond, acetoin, 172 303,525 amide activation, 192 alkylcobaloximes, 303, 364 amide deamination, 191 alkylcobalt complexes, cobalt-carbon amide hydrolysis, dinitrogen tetroxide, bond, 525,552 192 base-on, off, isopropylcobalamin, 552 m-anisidine, 172 3-bromopropylcobaloxime, 304 Arndt-Eistert, 194 carboxymethylcobaloxime, 304 Beckmann rearrangement, 180 chloromethylcobaloxime, 304 (+)camphor, ring C, 174, 184, 193 cobalt-carbon bond, /3-elimination, 304 camphorquinone, 183 cyanome hylcobaloxime, 304 Claisen rearrangement, amidoacetal, 184 cyclohexylcobaloxime, 304 cobyric acid, 187, 196 kinetics, isopropylcobalamin, 552 coupling, east and west halves, 187 methylcobalamin, 303, 363 cyanobromide, 1, 172 neopentylcobalamin, homolytic cleavage, cyclic 2',3', a-ribazole phosphate, 194 364,552 cyclohexyl nitrone, 192 1-phenylethylcobaloximes, 304 diazomethane esterification, basic a-styrylcobaloxime, 304 conditions, 193 Thioamide alkylation, vitamin B12 total Diels-Alder, Lewis-acid catalyzed, 183 synthesis, 195 the eastern half, 183 Thiocyanatocobalamin, electronic spectrum, episulfides, 185 411 ester ammonolysis, 192 Thiolactam, vitamin B 12 total synthesis, Hagemann's ester, 184 185 high pressure liquid chromatography, Thiolactone, desulfurization, decarbonyla- 190 tion, vitamin B12 total synthesis, isoxazoles, 175 193 methylmercury isopropoxide, 185 Thiols: neocobyric acid, 187, 196 alkylcobalamins, 527 nitrile, hydrolysis, 191 alkylcobaloximes, dealkylation, 527 orbital symmetry, 176 cobalt-carbon bond reductive cleavage, orthoamide, 178 515 oxime hydrolysis, nitrous acid, 170

Total synthesis of vitamin B12 (Cont'd) Trifluoromethylcobalamin, reaction with ozonolysis, 174 cyanide, 307 a-phenylethylamine, resolving agent, Trifluoromethylcobaloxime, reaction with 183 hydroxide, cob(I)aloxime, 309 (-)-a-phenylethyl isocyanate, 173 1-(2-Trifluoromethylphenyl)imidazole, photochemical path, 192 heptamethylcobyrinate coordina- regiospecific aldol, 179 tion, 495 retro-Claisen, 174 p-Trifluoromethylphenyl(pyridine)cobalo- b-ribazole, 198 xime, preparation, 271 D-ribose, 198 3,3,3-Trifluoropropyne, addition to cobalt ring closure, 190, 196, 197 (I) complexes, 257 rings A-D, 172 Trimethylaminoethylcobalamin, reaction rings B-C, 183 with alkali, 310 secocorrins, 196 Trimethylated isobacteriochlorins: stereospecific thermal cyclization, 176 biosynthesis, 132 sulfur extrusion reactions, 185, 190 electronic spectrum, octamethyl ester, 132 template reactions, 188 incorporation into, cobyric acid, 132 tetracyclic lactam, 174 isolation, 132 thioamide alkylation, 195 nmr spectrum, 132 thiolactam, 185 from P. shermanii, 132 thiolactone, desulfurization, decarbonyla tion , 193 structure, 132, 134 tricyclic ketone, 173 Triphenylphosphine cob(II)aloximes, alkyl Transalkylation, cobalt(I) complexes by halides, reactivity towards, 521 alkylcobalt(III) complexes, 527 Transcobalamin-II, 156 Unique biologically, redox chemistry of rrafts-dimethylcobalt(III) complexes, cobalt, 340 heavy metal alkylation, 527 Unsaturated electrophiles, cobalt(I) com- trans-effect: plexes, addition to, 256 cobaloximes, 82 Uro'gen III, see Uroporphyrinogen III corrin, 80, 330 Uroporphyrin I, structure, 118 ligand ordering, 346 Uroporphyrin III, structure, 110 nephelauxe ic series, 336 Uroporphyrinogen I, interaction with nmr spectroscopy: cosynthetase, 118 cobalt complexes, 488 Uroporphyrinogen III: corrin, 487 biosynthetic precursor, cobyrinic acid, 5,6-dimethylbenzimidazole, 488 116 methylcorrinoids, 489 corrin biosynthesis, 139 spectrochemical series, 336 intact incorporation into corrin, 117 Transmission, corrin steric effects, 355 loss of C-20 in corrin biosynthesis, 137 Trichloromethylcobalamin photolysis, 303 structure, 110

Tricyclic ketone, vitamin B 12 total synthesis, Uroporphyrinogen III cosynthetase, 117 173 uroporphyrinogen I in teraction with, 118 Tricyclohexylphosphincobal(II)Oxime Uv spectrum, see Electronic spectrum alkyla ion, alkyl halides, 519 Trie hylaminoethylcobalamin, reaction with Vibrational components, electronic c yanide, 307 spectrum, 403 Trifluoroacetic acid: Vinylcobalamin: corrin epimerization, 222 electronic spectrum, 346, 415 59 epimerization, neocorrinoids, 222 nmr spectrum ( Co), 490

vitamin B12 , reaction with, 223 eaction with acid, 314 Trifluoroethylcyanocobalamin, electronic Vinylcobaloxime preparation, 261 spectrum, 413 Vinylcobalt porphyrins, diazoalkanes, preparation, 280

Vinylcobinamide electronic spectrum, 408 cobalt: Vinylcyanocobalamin, electronic spectrum, incorporation into, 211 413 reduction by alkali, 226 Vinyl ethers: role in, 333, 335 cob(III)aloxime alkylation, 281 cobyric acid, conversion to, 197 cobalt(III) complexes, reaction with, 281 cobyrinic acid, acid hydrolysis, 230 hydroxocobalamin alkyla ion, 281 color and clinical activity, 8 Vinyl halides, alkylation cobalt(I) complexes, comparison (crystallographic) with

stereochemistry, 260 vitamin B 12 coenzyme (table), Vinyl(pyridine)cobaloxime cobalt-carbon 53 bond, bond lengths, 505 comparison to model systems, 504 Vinyl(pyridine)Z>w(salicylaldehyde)ethylene- conjugated system, 238 diiminecobalt cobalt-carbon bond, conversion to: bond lengths, 505 15-carboxy-15-norcobinamide, 239 Visible spectrum, see Electronic spectrum cobinamides, 234

Vitamin B 12: cobyric acid, 235 absolute configuration, 28 dicyanocobalamin, standard electronic acetamide side chain, 30 spectrum, 395 acid hydrolysis, 230, 232, 234 heptamethyl dicyano-5,15-bisnorco- addition of chlorine, 216 byrinate, 239 air dried crystals, 25 heptamethyl dicyanocobyrinate, 236 amide side chain, nomenclature, 19, 30 pentadecaalkylcorrin, 236 animal protein factor, 14 coordination chemistry, 325-392 antipernicious anemia factor, 11 copper, incorporation into, 211 aromaticity, 204 copper analog, 211 biosynthesis: corrin, pentadecaalkyl from, 236 [5-13C]-aminolevulinic acid, 479 crystal morphology: 13 [ CH 3 ] -L-methionine, 480 pleochroism, 26 nmr spectroscopy, 28, 107, 479 refractive index, 26 [8-13C] porphobilinogen, 480 cyanation, 213 bond angles (tables), 45-53 cyanocobalamin, 17 bond distances (tables), 45-53 dehalogenation, 217 bound to intrinsic factor, electronic demetallation, 210 spectrum, 414 dependent, table: bromination, 215 isomerase reactions, 328 buckling, 208 mutase reac ions, 328 canonical resonance structures, 205 deuteration, 212 carboxylic acids, preparation, 231 5,6-dichlorobenzimidazole, X-ray cell dimensions, 93 diffrac ion data, 27 cerium(III) hydroxide, cobinamide dimethylaminomethylation, 213 from, 236 electronic spectrum, 207, 393-430, chemical degradation, 111 408,413,415,417 chemical formula, 28, 93 film, 343 chirality, 170 electrophilic attack, MO-calculations, 212 chloramine T, reactions, 215 epimers, C-3, C-8, C-13, 210 chlorination, electronic spectrum, from fermentation, 9 215 ferredoxin, decyanation, 163 chromatography, acid hydrolysis first crystallization, 3 products, 230 fluorescence, 426 chromic acid oxidation, 218 halogenation, c/s-effect, 216, 226 circular dichroism, 223, 420 helicity, 209 cobaloximes, X-ray crystallography, hexacarboxylic acid: 23-106 bond angles (tables), 45-53

Vitamin B 12 (Cont'd) chemical shifts, 485 bond distances (tables), 45-53 (13C) table, 476 cell dimensions, 92 longitudinal relaxation times, 485 chemical formula, 92 praseodymium, 484 deuteration, 212 Nobel prize, 2 electronic spectrum, 417 nomenclature, 17-22 folding, 60 numbering (nomenclature), 18 space group, 92 optical rotatory dispersion, 223 structure, 28, 204 orbital energies, 206 torsion around A-D junction, 57 organic solvent soluble, 236 X-ray crystallographic data, 92 organometallic chemistry, 326 X-ray diffraction data, 27 ozonolysis, 218 history, 1 pentacarboxylic acid, electronic spectrum, hydrolysis, side chain, amide, 33 417 infrared spectrum, 215 peripheral amide groups, reactions, 230- 7-irradiation, frozen solution, 318 234 isolation, 3, 24 permanganate oxidation, 218, 239 lactam: pernicious anemia, 1 electronic spectrum, 417 5'-phosphate: formation, 225, 234 bond angles (tables), 45-53 X-ray structure (diagram), 42 bond distances (tables), 45-53 lactone: cell dimensions, 94 electronic spectrum, 417 chemical formula, 94 formation, 226 planarity deviations, 61 c-lactone structure, 227 space group, 94 laser Raman spectrum, 343 structure, 34 luminescence, 426 torsion around A-D junc ion, 57 metal-free, 211 X-ray crystallographic data, 94 metal replacement, 72 X-ray structure (diagram), 34 methanolysis, 236 photolysis, 404 raeso-methyl groups: planarity deviations, 61 oxidation, 239 polarization effects, 402

pKa values, 234 precursor, vitamin B12 coenzyme, 163 microbiological assay, 7 preparation, 215 monocarboxylic acid: propionamide side chain, 30 bond angles (tables), 45-53 pulse radiolysis, 318 bond distances (tables), 45-53 pyrolysis, 239 cell dimensions, 93 reaction with: chemical formula, 93 ascorbic acid, 229 nmr spectrum, 486 iodine, 226 space group, 93 trifluoroacetic acid, 223 structure, 34 redox chemistry, model systems, 513 torsion around A-D junc ion, 57 rhodium, incorporation into, 211 X-ray crystallographic data, 93 rhodium analog, 211 monocarboxylic acid (E2): selenocyanide neutron diffraction, 33 selenium location, 27 X-ray diffraction data, 33 X-ray diffraction data, 26 X-ray structure (diagram), side chain side chain conformations, 208 disorder, 33 solvent effects, table, electronic spec- nitrosation, 217 trum, 410 nmr spectrum: space group, 93 13C, biosynthetic studies, 112 steric crowding, 506 13C-enriched, 471, 472, 474, 480 structure, 24, 170

Vitamin B 12 (Cont'd) laser Raman spectrum, 343 meso-substitution, 212 low spin Co(II), 432

succinimides ; oxidative cleavage, 217 methylcobalamin photolysis, 300 torsion around A-D junction, 57 methyl radicals: total synthesis, see Total synthesis, recombination, 553

vitamin B 12 scavenger, 300 water of crystallization, 68 nmr spectrum, 487 wet crystals, X-ray diffraction data, 25 nomenclature, 18 X-crystallographic comparison, wet and organic radical interaction: air-dried, 67 epr spectrum enzymic reaction, 450 X-ray crystallographic data, 93 separation, 452 X-ray diffraction data, 26 oxidation, organic radicals, 376 X-ray structure (diagram), 31, 32 oxygenation, epr spectrum, 458 yellow corrinoids, preparation, 228-230 oxygen complex, structure, 459 zinc, incorporation into, 211 paramagnetic shifts, nmr spectrum, 487 zinc analog, 211 preparation, 439 see also Corrin; Cyanocobalamin; pulse radiolysis, 318 14 Neovitamin B12 N quadrupole interaction, 441

Vitamin B 12s : radical recombination, 363 reduction, zinc/acetic acid, 365 rate, organic radical recombina ion, 525 see also Hydroxocobalamin reaction with alkyl halides table , 274

Vitamin B 12b , see Hydroxocobalamin reduction, organic radicals, 376

Vitamin B 12r- reduction of vitamin B12 , ribonucleotide alkylation: reductase, 434 alkyl halides, 520 reductive cleavage, alkylcobalamins, 317 radical intermediates, 520 spin-Hamiltonian, table, 441 synthetic utility, 277 steric interactions, epr spectrum, 442, alkyl halides, reactivity toward, 521 448 base-on, off, epr spectrum, 299 substrate radical separation, table, benzyl bromide, reaction with, 513 ethanolamine ammonia- binding to, ribonucleotide reductase, lyase, 454

442 vitamin B 12 coenzyme, enzymic reaction, p-bonding, 440 530

complex with iodide, 522 vitamin B128, 514 5'-deoxyadenosyl radical, reaction with, X-ray crystallographic data, 69 373 see also Cob(II)inamides; Cobalt(II)com-

disproportionation, vitamin B 128, 253, plexes 514 Vitamin B 12s: electronic spectrum, 418 acetylcobalamin, alkali, 311 ENDOR,441,442 acidity, 253 enzymic formation, 157 adenosine triphosphate, vitamin B12 epr spectroscopy: coenzyme biosynthesis, 523 monoclinic model, 440 alkylation: powder samples, 439, 442 alkyl halides, 523 principal axes, 440 kinetics, 259 single crystals, 442 stereochemistry, 260, 523 epr spectrum, oxygenated, 434, 439, alkylcobalamins, photolysis, 302 458 assay, vitamin B 12 coenzyme bio- formation, Lactobacillus leichmanni, synthesis, 156-161 ribonucleotide reductase, 439 benzyl bromide, reaction with, 513 intermediate: coenzyme function, 147 enzymic reaction, 381 cyclodecyl-l-d-iodide, reaction with, interaction with substrate radicals, 382 261

Vitamin B 12s (Cont'd) bond angles, tables, 45-53 5,6-dimethylbenzimidazole, coordina- bond distances, tables, 45-53 tion, 486 capped cobaloximes, model systems, dimethyl(bromomethyl)malonate, 533,565 reaction with, 564 cell dimensions, 93 electronic spectrum, 418 chemical formula, 93 enzymic formation, 158 circular dichroism, 421 isopropylcobalamin, ^-elimination, cleavage, cobalt-carbon bond, 547-554 364 cobalamins, conversion to, 156 2',3'-isopropylideneadenosy lcobalamin cobalt-carbon bond: and r-butoxide, 307 bond lengths, 505 laser Raman spectrum, 343 bond strength, 513 methylation, N5 -methyltetrahydrofolic cleavage, induc ion, 550 acid, 528 model systems, 551 nmr spectrum, 486 factors affecting bond dissociation nomenclature, 18 energy, 531 nucleophilicity, 251, 523 models for cleavage, 551 photolysis, cobalt-carbon bond, 297 protection by side chains, 30, 41 pK values, 364 comparison to model systems, 504 protonation, 364 conformation, 551 reaction with aryl halides, 271 conformational changes, 374 b-substituted alkylcobalamins and constraint of axial ligands, 41 alkali, 310 conversion to methylcobalamin, 163

vitamin B 12 coenzyme, 549 5- and 6-coordinate, 346

vitamin B 12r, disproportionation, 514 cyanide, D-eo>f/zro-2,3-dihydroxy-4-

vitamin B 12s, 514 pentenal, 305 see also Cob(I)inamide; Cobalt(I)com- 5'-deadenosyl carbanion and elimination, plexes; Hydridocobalamin cobalt-carbon bond, 549

Vitamin B 12 coenzyme: 5'-deadenosyl carbocation, cobalt-carbon acid, cobalt-carbon bond cleavage, 312 bond,548 acid decomposition: 5'-deadenosyl radical, cobalt-carbon cobalt-carbon bond, 366 bond, 548 2,3, dihydroxy-4-pentenal, 312 5'-deoxyadenosine, intermediate, 332, adenosyl carbene, 549 545 alkaline decomposition, cobalt-carbon 5-deoxyadenosyl ligand, 13C-5'- bond,366 deriva ive, 268 alkylcobalt complexes, model systems, 5'-2H-deoxyadenosyl ligand, nmr 551,564 spectrum,471 aminomutases: m-diaminoplatinum(II), coordination, model systems, 571 497 reaction pathways, 573 iol dehydrase: analogs, 5'-deoxy-5'-halonucleosides, 1,2-dihydroxyalkyl radicals, 571 preparation, 267, 551 model systems, 571 base-on, off, electronic spectrum, 350, dissociation, 472 357 electrocyclic ring opening, enzymic biosynthesis: reaction, 576 eukaryotes, 156 electronic spectrum: prokaryotes, 156 calculations, 398,408

vitamin B 128: film, 343, 350 adenosine triphosphate, 523 enzyme bound, 554 assay, 145-167 enzymic reaction, table, 546 bis(salicylaldehyde)ethylenediimineco active site thiol, 555 balt(III), - cobalt-carbon bond cleavage, 507 model systems, 551

VitaminB12 coenzyme (Cont'd) olefin p-complexes, 571 cobalt role, 555 reaction pathways, 571 cobalt(II) substrate radical separation, halogenation, 216 452 heterolytic cleavage, cobalt-carbon 5'-deoxyadenosyl radical, 554 bond,548 diol dehydrase, 529 hexacarboxylic acid, X-ray structure, dissociation-recombination pathway, 31,32 555 1 H/2 H exchange, nmr spectrum, 468, epr spectroscopy, 449-458, 558 469 ethanolamine ammonia-lyase, 529 homolytic cleavage, cobalt-carbon glutamate mutase, 529 bond,548 hydrogen abstraction, 554 1,2-hydride shift, 549 hydrogen exchange, 449 hydridocobalamin, 549 13C intermediates, epr spectrum, 450 hydrophobic pocket, 41 2H intermediates, epr spectrum, 450 Iodine, cleavage, 316 kinetic isotope effect, 554 gamma-irradiation, frozen solution, 318 2 methyImalonyl-CoA mutase, 529 kinetic isotope effect, [ I- H2 ] propane- MO-calculations, 557 1,2-diol, 554 model systems, 501-541, 528-535, labelled 2H, 3H, 545 564-577 lactam formation, 226 oxidative addition, 576 laser Raman spectrum, 343 protein role, 555 mechanism, role of model systems, 528 radical doublet intermediates, 450 mechanism of action: rapid reaction intermediate, 455 model systems, 543-582 reaction pathways, 555 theory, 543-582 reversibility, 545 methylcobalamin, conversion to, 163 ribonucleotide reductase, 529 a-methyleneglutarate mutase: theoretical studies, 557 model systems, 567

vitamin B 12r as intermediate, 530 reaction pathways, 570 enzymic reactions: methylmalonyl-CoA mutase: a-bonded organocorrinoids, 547 mechanism, 565 cobalt-carbon bond cleavage, 547 model systems, 564 electron transfer, 547 reaction pathways, 565, 566 hypothetical pathways, 547 migration of group X, electron transfer, organic radicals, 547 555 enzymic role, olefin n-complexes, 534 model systems: epr signals during catalysis, 332 5,7,7,12,14,14-hexamethyl-l,4,8,ll- ethanolamine ammonia-lyase: tetraazacyclotetradeca-4,11- model systems, 571 dienecobalt, 377, 501-541, 574 olefin ^-complexes, 575 ligand binding, 504 radical ca ions, 573 pKa values, 504 reaction pathways, 573 redox chemistry, 504 flash photolysis, electronic spectrum, redox potential, 504 299,376 bis(salicylaldehyde)ethylenediimine- fluorescent analogs: cobalt, 551 2-aminomebularine, 267, 285, 300 1,4,8,11-tetraazacyclotetradecane, 551 2,6-diaminobularine, 300 molecular rearrangements, 545 6 1,N -ethenadenosine, 300 neutron diffraction, 91 formycin, 300 nitrosodurene, reaction with, 298 glutamate mutase: nmr spectroscopy, 465 acrylate radical, 571 nmr spectrum: glycinyl radical, 571 chemical shifts, 465 model systems, 570 corrin ring, 469

VitaminB12 coenzyme (Cont'd) steric crowding, 506 5'-deoxyadenosyl ligand, 468 steric effects, ligand equilibria, 341 5,6-dimethylbenzimidazole, 468, 474 strain orbital, 560

praseodymium, 483 structural comparison to vitamin B 12, 41 propanolamine, 467 structure, 19, 25 protonated, 468 substrate radicals, 382 ribose ring, 467 synthe ic analogs, 332 nomenclature, 18 1,4,8,11-tetraazacyclo tetradecane- nucleoside analogs, 160 cobalt(III), model, 551 olefin 7r-complexes, 549, 575 thiols, photolysis, 5'-deoxyadenosine, organic radicals, 545 299 oxygen sensitivity, 551 torsion around A-D junction, 57

peripheral amide groups, 41 vitamin B 12: photolysis: comparison (crystallographic) with, 53 acetaldehyde: precursor, 163

ethanolamine, 298 vitamin B 12s, 549 2-ethoxyethylamine, 298 X-ray crystal structure, 550 ethylene glycol, 298 X-ray diffraction data, 30, 93 electronic spectrum, 296 X-ray structure, 31, 32, 43, 44 frozen solution, epr, 299 see also Alkylcobalamins model for e hanolamine ammonia- lyase, 298 Wagner-Meerwein rearrangement, organic in presence of nitrosodurene, 298 radicals, 556

in presence of thiols, 298 Water of crystallization, vitamin B12, 68 quantum yield, 296, 303, 363 Work up of reaction mixtures, cobalt- pK values, benzimidazole, 351 carbon bond synthesis, 248 planarity deviations, 61 protein role, distortion, 373 Xan hocorrinoids: protonated, nmr spectrum, 468 corrin cyclization (peripheral), 225- protonation, 351 230 pulse radiolysis, 318 see also Yellow corrinoids purine nucleosides, 300 X-ray crystallographic comparison, wet

ratio, methylcobalamin, 161 and air-dried vitamin B 12 , 25, 67 reaction with: X-ray crystallographic data, corrin derivative alkali, 307 derivatives, 23-106 cyanide, 305 X-ray crystallography: a,|3-dibromoethyl acetate, 285 R-a-cyanoethyl(S-a-methylbenzylamine)- hydrogen cyanide, 306 cobaloxime, racemization, 88 redox chemistry, model systems, 513 glossary, 97

ribonucleotide reductase: vitamin B 12, cobaloximes 23-106 5'-deoxyadenosine, 577 see also X-ray structure 5'-deoxyadenosyl radical, 577 X-ray structure: thiyl radical, 577 alkylcobaloximes, 359 ribose ring conformation, 550, 554 anomalous dispersion, 99 ring puckering, 41 cylindrical projection, 55, 100 role of protein, 329 difference electron density map, 99 solvent effects, table, electronic spectrum, direct methods, 99 410 electron density map, 100 space group, 93 methylcobalamin, complex with bis- spin-labelled analogs, 267 acetylacetone-ethylenediamine, 349

spin-lattice relaxation times, 492 neovitamin B 12 , 34, 36 stability cobalt-carbon bond, 366 nmr spectroscopy, molecular structure steric compression, X-ray structure, 359 in solution, comparison to, 482

X-ray structure (Cont'd) nmr spectrum, 229, 485 Patterson map, 98, 101 13C nmr spectrum, 229 R factor, 99 planarity, deviations, 61

rhodium coby rinic acid- tf ,c-diamide, 34 preparation, vitamin B 12 , 228-230

side chain disorder, vitamin B 12 mono- radical reactions, vitamin B12, 229 carboxylic acid (E2), 33 ring structure, 37

vitamin B 12: space group, 94, 95 lactam, 40 structure, 37-40, 228-230 5'-phosphate, 31, 32, 34 torsion around A-D junction, 57

vitamin B 12 coenzyme: X-ray diffraction data, 37, 94, 95 hexacarboxylic acid, 31, 32 X-ray structure, diagram, 38 steric compression, 31, 32, 43, 44, 359 Zinc: yellow corrinoids, 38 alkylation, trans-dimethylcobalt(III) complexes, 527 Yellow corrinoids: cobalamin reduction, 253 ascorbic acid, role in formation, 39, incorporation into: 229 15 -cy ano-1,2,2,7,7,12,12-hep ta- bond angles, distances, tables, 45-53 methylcorrin, 211

cell dimensions, 94, 95 vitamin B 12, 211

chemical formula, 94, 95 Zinc/acetic acid, vitamin B123 reduction, dehydration, 229 365

folding, 60 Zinc analog, vitamin B 12 , 211 gCoPSE: Zinc 15 -cyano-2,2,7,7,12,12-hexamethy 1- preparation, 40 corrin: structure, 42 electronic spectrum, 424 X-ray diffrac ion data, 40 structure, 423 mechanism of formation, 229 Zwitterionic: microbiological formation, 228 cobalt(III) complexes, 286