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The Chemistry and Biochemistry of Vanadium and the Biological Activities Exerted by Vanadium Compounds

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The Chemistry and Biochemistry of Vanadium and the Biological Activities Exerted by Vanadium Compounds Chem. Rev. 2004, 104, 849−902 849 The Chemistry and Biochemistry of Vanadium and the Biological Activities Exerted by Vanadium Compounds Debbie C. Crans,* Jason J. Smee, Ernestas Gaidamauskas, and Luqin Yang Department of Chemistry, Colorado State University, Fort Collins, Colorado 80523-1872 Received June 6, 2003 Contents 4.2. Ribonuclease 866 4.2.1. Structural Characterization of Model 867 1. Introduction 850 Compounds for Inhibitors of Ribonuclease 2. Aqueous V(V) Chemistry and the 851 − 4.2.2. Characterization of the 867 Phosphate Vanadate Analogy Nucleoside-Vanadate Complexes that 2.1. Aqueous V(V) Chemistry 851 Form in Solution and Inhibit Ribonuclease 2.2. Mimicking Cellular Metabolites: 852 4.2.3. Vanadium−Nucleoside Complexes: 868 Vanadate−Phosphate Analogy Functional Inhibitors of Ribonuclease (Four-Coordinate Vanadium) 4.3. Other Phosphorylases 868 2.3. Structural Model Studies of Vanadate Esters 852 4.4. ATPases 869 2.4. Vanadate Esters: Functional Analogues of 853 4.4.1. Structural Precedence for the 869 Phosphate Esters Vanadate−Phosphate Anhydride Unit: 2.5. Vanadate Anhydrides: Structural Analogy 854 Five- or Six-Coordinate Vanadium with Condensed Phosphates 4.4.2. Vanadate as a Photocleavage Agent for 870 2.6. Potential Future Applications of 855 ATPases Vanadium-Containing Ground State Analogues in Enzymology 5. Amavadine and Siderophores 871 3. Haloperoxidases: V(V) Containing Enzymes and 855 5.1. Amavadine 871 Modeling Studies 5.1.1. Amavadine: Structure 871 3.1. Bromoperoxidase 855 5.1.2. Amavadine: Activities and Roles 872 3.2. Chloroperoxidase 856 5.2. Siderophores 873 3.3. From Haloperoxidases to Phosphatases 857 5.2.1. Effects of Vanadium on 873 3.4. Structural Modeling Studies of the 857 Siderophore-Mediated Iron Transport 5.2.2. Characterization of 874 Vanadium-Dependent Haloperoxidases − 3.5. Spectroscopic Modeling Studies of the 859 Vanadium Siderophore Complexes and Vanadium-Dependent Haloperoxidases Model Complexes 3.6. Functional Modeling of the 860 5.2.3. Vanadium Citrate Complexes: Structure 874 Vanadium-Dependent Haloperoxidases and Speciation 3.7. Oxidation of Sulfides by Haloperoxidases 860 5.2.4. V(V) and V(IV) Hydroxamate Complexes 875 (VHPOs) 6. Tunicates and the Polychaete Fan Worm 876 4. Inhibition of Phosphorylases by V-Compounds: 861 6.1. Tunicates 876 Phosphatases, Ribonuclease, Other 6.1.1. Location of Vanadium in Tunicate Blood 877 Phosphorylases, and ATPases Cells 4.1. Phosphatases 861 6.1.2. Aqueous V(III) Chemistry 877 4.1.1. Vanadate: An Imperfect Transition State 861 6.1.3. Oxidation State of Vanadium in Tunicates 878 Analogue of Phosphatases 6.1.4. Uptake of Vanadate into Tunicates 879 4.1.2. V(IV) Chemistry and Inhibition of 862 6.1.5. Vanadium Binding Proteins: Vanabins 879 Phosphatases by V(IV) 6.1.6. Model Complexes and Their Chemistry 880 4.1.3. Inhibition of Alkaline and Acid 864 6.1.7. Catechol-Based Model Chemistry 880 Phosphatases by Vanadium Compounds 6.1.8. Vanadium Sulfate Complexes 881 4.1.4. Inhibition of Protein Phosphatases by 864 Vanadium Compounds 6.2. Fan Worm Pseudopotamilla occelata 883 4.1.5. Inhibition of Purple Acid Phosphatases by 865 7. Vanadium Nitrogenase 883 Vanadium Compounds 7.1. Nitrogenases 883 4.1.6. Phosphatase and Other Phosphorylase 866 7.2. Biochemistry of Nitrogenase 884 Inhibition by Oxometalates 7.3. Clusters in Nitrogenase and Model Systems: 885 4.1.7. Structural Models of the Transition State 866 Structure and Reactivity of Phosphate Ester Hydrolysis 7.4. Structural Model Complexes of the VFe 886 Cofactor Binding Site * To whom co rrespondence should be addressed. Phone: 970-491- 7.5. Homocitrate 887 7635. Fax: 970-491-1801. E-mail: [email protected]. 7.6. Activation of Nitrogen 887 10.1021/cr020607t CCC: $48.50 © 2004 American Chemical Society Published on Web 01/29/2004 850 Chemical Reviews, 2004, Vol. 104, No. 2 Crans et al. 7.7. Formation of Hydrazine and Other Reduced 888 Compounds 8. Additional Focus Areas in Biomimetic Vanadium 888 Chemistry 8.1. Peroxidase Activity of Vanadium Compounds 888 8.2. Catalase Activity of Vanadium Compounds 889 8.3. Vanadium Porphyrins 889 8.4. Insulin-Like Effect of Vanadium Compounds 889 8.5. Affinity for Transport Proteins: Transferrin 891 and Serum Albumin 8.6. Newly Discovered Class of 892 Vanadium-Containing Enzyme 9. Summary 892 10. Acknowledgments 892 11. List of Abbreviations 892 Debbie C. Crans did her undergraduate work at the University of 12. References 893 Copenhagen, Denmark, where she was born. She came to the United States for the first time in 1975 to Washington State University as a Danish exchange student. She returned to the United States in 1980 as a Ph.D. student at Harvard University, and did her postdoctoral studies at the 1. Introduction University of California, UCLA. She is a Professor in Organic and Inorganic Chemistry at Colorado State University where she began teaching in 1987. Vanadium is a trace element, which may be ben- Her research interests include bioinorganic chemistry, with a particular eficial and possibly essential in humans1 but certainly interest in vanadium chemistry, biochemistry, and applications in enzymol- essential for some living organisms.2-11 Metal ions ogy. She is married to Christopher R. Roberts and is the mother of three and thus vanadium ions can play a role in biology as daughters, Patricia Crans Roberts (8), Gerri Marie Roberts (8), and Mia counterions for protein, DNA, RNA, and in various Crans Roberts (3). In 1997, she co-organized the first symposium in “Vanadium Chemistry and Biochemistry” and is presently the Program biological organelles. The structural role is often Chair for the Inorganic Chemistry Division of the American Chemical manifested by the maintenance of various biological Society. structures, whereas a functional role is to bring key reactivity to a reaction center for a protein. Vana- dium ions have many structural roles reflected by its structural and electronic analogy to phosphorus.9,12-20 In addition, the vanadium ion is an enzyme co- factor,7,9,21-30 and is found in certain tunicates4-11,16 and possibly mammals.1 Reviews on how vanadium can act and function in the biosphere include inves- tigations into the fundamental coordination and redox chemistry of the element,16-18,29,31-35 as well as structural and functional aspects of biological sys- tems and/or metabolites.12,36 Modeling biological ac- tivities of various types have long been of interest to chemists, with this discipline focusing on the struc- tural modeling until about a decade ago when the focus shifted to functional modeling. Clearly modeling that includes both aspects will be most informative, Jason J. Smee received his B.Sc. at Kansas State University in 1994. He then pursued a Ph.D. under the direction of Marcetta Y. Darensbourg and the ultimate goals for model chemists. Although at Texas A&M University in College Station, Texas. After graduating in the latter in general may be of greater interest at 2000, he moved on to Colorado State University where he is a postdoctoral the present time, the structural aspects of the various associate with Debbie C. Crans. His research focuses on the synthesis oxidation states are defining its effects in many and characterization of novel vanadium complexes as potential therapeutic biological systems. In this review, we have combined drugs in the treatment of diabetes. In his spare time he enjoys reading, the two fundamentally different aspects of modeling playing softball, and long bike rides. because the coverage of only one of these areas in nistic studies revealing how the enzyme-catalyzed our opinion would not provide the reader the proper reaction takes place,7,22,23,37,38 to the design of simple sense of the effects and activities exerted by vana- vanadium complexes (V-complexes) exhibiting simi- dium compounds (V-compounds). lar activities as the enzyme show how much the This review describes the voyage from the discov- chemists can do.7,9,29,38,44-48 Inhibition of phosphatases ery of the first vanadium-containing enzymes in by V-compounds is firmly established,9,12-15,19,20 and 1984, haloperoxidases,7,9,21-26,37,38 to the current X-ray often the versatility of the vanadium to bind as a crystallographic studies; it is a fascinating story that four-coordinate ground state analogue and a five- provides inspiration to chemist in many fields. These coordinate transition state analogue is not generally studies map out the enzyme active site24,39-43 and recognized; thus, V-compounds can act as substrates demonstrate the structural and functional link be- although bioinorganic chemists are more familiar tween apohaloperoxidases and certain phospha- with the five-coordinate transition state analogy as tases.24,39-43 These discoveries now give the bioinor- exemplified in the potent inhibition of phosphatases, ganic chemists clear directives. The detailed mecha- ribonuclease,49,50 and other phosphorylases. Although Chemistry and Biochemistry of Vanadium Chemical Reviews, 2004, Vol. 104, No. 2 851 V-compounds and the multitude of reactions they can catalyze or affect through structural analogy. The topics in this review have been organized according to oxidation state of the metal in a par- ticular system, since the oxidation state of the vanadium ion is important to the species that direct the chemistry that can occur16-18,29,31-35 in the reac- tions. After initially describing the V(V) chemistry, the areas in the biosphere associated with V(V) haloperoxidases and potent inhibition of phosphory- lases will be reviewed. This is followed by the V(IV)- containing amavadine and vanabins. The tunicates and the polychaete worm contain both vanadium (IV) and (III) depending on the species. The oxidation state of vanadium in the metal clusters of the Ernestas Gaidamauskas, born in 1971 in Vilnius, Lithuania, received his nitrogenase is less obvious but generally believed to Ph.D.
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