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JOURNAL of BACTERIOLOGY VOLUME 169 DECEMBER 1987 NUMBER 12 Samuel Kaplan, Editor in Chief (1992) Kenneth N

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JOURNAL OF BACTERIOLOGY VOLUME 169 DECEMBER 1987 NUMBER 12 Samuel Kaplan, Editor in Chief (1992) Kenneth N. Timmis, Editor (1992) University of Illinois, Urbana Richard M. Losick, Editor (1988) Centre Medical Universitaire, James D. Friesen, Editor (1992) Harvard University, Cambridge, Mass. Geneva, Switzerland University of Toronto, L. Nicholas Ornston, Editor (1992) Graham C. Walker, Editor (1990) Toronto, Canada Yale University, New Haven, Conn. Massachusetts Institute of Stanley C. Holt, Editor (1987) Robert H. Rownd, Editor (1990) Technology, Cambridge, Mass. The University of Texas Health Northwestern Medical School, Robert A. Weisberg, Editor (1990) Science Center, San Antonio Chicago, Ill. National Institute of Child June J. Lascelles, Editor (1989) Health and Human University of California, Los Angeles Development, Bethesda, Md. EDITORIAL BOARD David Apirion (1988) James G. Ferry (1989) Eva R. Kashket (1987) Palmer Rogers (1987) Stuart J. Austin (1987) David Figurski (1987) David E. Kennell (1988) Barry P. Rosen (1989) Frederick M. Ausubel (1989) Timothy J. Foster (1989) Wil N. Konings (1987) Lucia B. Rothman-Denes (1989) Barbara Bachmann (1987) Robert T. Fraley (1988) Jordan Konisky (1987) Rudiger Schmitt (1989) Manfred E. Bayer (1988) David I. Friedman (1989) Dennis J. Kopecko (1987) June R. Scott (1987) Margret H. Bayer (1989) Masamitsu Futai (1988) Viji Krishnapillai (1988) Jane K. Setlow (1987) Claire M. Berg (1989) Robert Gennis (1988) Terry Krulwich (1987) Peter Setlow (1987) Helmut Bertrand (1988) Jane Gibson (1988) Lasse Lindahl (1987) James A. Shapiro (1988) Terry J. Beveridge (1988) Robert D. Goldman (1988) Jack London (1987) Louis A. Sherman (1988) Donald A. Bryant (1988) Susan Gottesman (1989) Sharon Long (1989) Howard A. Shuman (1988) Joseph M. Calvo (1987) E. Peter Greenberg (1988) Paul S. Lovett (1987) Issar Smith (1987) A. M. Chakrabarty (1989) Scott R. Hagedorn (1988) Ben J. J. Lugtenberg (1989) John L. Spudich (1988) Keith F. Chater (1988) Barry G. Hall (1988) Robert Macnab (1988) Catherine Squires (1987) Terrence G. Cooper (1987) R. E. W. Hancock (1987) Philip Matsumura (1989) Robert Switzer (1987) John E. Cronan, Jr. (1989) Richard S. Hanson (1988) Larry McKay (1987) Godfried D. Vogels (1987) Jorge H. Crosa (1988) Robert Haselkorn (1987) S. Mizushima (1988) Barry Wanner (1987) Walter B. Dempsey (1989) Gerald L. Hazelbauer (1987) Edward A. Morgan (1987) Bernard Weisblum (1989) Patrick Dennis (1988) Dennis Henner (1988) Gisela Mosig (1988) Malcolm Winkler (1988) W. Ford Doolittle (1988) Charles L. Hershberger (1987) Robert A. Niederman (1988) Peter A. Williams (1989) David A. Dubnau (1989) Penny J. Hitchcock (1987) Hiroshi Nikaido (1989) David Womble (1989) Martin Dworkin (1988) James Hopper (1988) Allen T. Phillips (1988) David R. Woods (1989) Alan D. Elbein (1989) Martha M. Howe (1987) Patrick J. Piggot (1987) Henry C. Wu (1987) Bert Ely (1988) Karin Ihler (1987) Barry Polisky (1987) Duane C. Yoch (1989) Wolfgang Epstein (1987) A. W. B. Johnston (1989) Linda Randall (1987) Howard Zalkin (1988) Helen R. Whiteley, Chairman, Publications Board Kirk Jensen, Director of Publications Linda M. Illig, Managing Editor, Journals Sara Joslyn, Production Editor The Journal of Bacteriology (ISSN 0021-9193), a publication of the American Society for Microbiology, 1913 I St., NW Washington, DC 20006, is devoted to the advancement and dissemination offundamental knowledge concerning bacteria and other microorganisms. Instructions to authors are published in the January issue each year; reprints are available from the editors and the Publications Department. The Journal is published monthly, one volume per year. The nonmember subscription price is $340 per year; single copies are $25. The member subscription price is $41 (foreign, $56 [air drop shipping]) per year; single copies are $8. 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T., 5379 Anderson, Julia M., 5579 Fayet, Olivier, 5641 Matsuhashi, Michio, 5692 Shapiro, Mary K., 5496 Arieli, Boaz, 5466 Ferenci, Thomas, 5339 Matsuyama, Kenji, 5815 Shimizu-Kadota, Mariko, 5481 Arlat, Matthieu, 5626 Ferreira, L. C. S., 5776 Matsuzawa, Hiroshi, 5692 Shinagawa, Hideo, 5429 Armitage, Judith P., 5801, Feucht, Brigitte U., 5416 Matzanke, Berthold F., 5873 Silhavy, Thomas J., 5339 5808 Flores, Margarita, 5782 McConnell, David J., 5766, Silver, Richard P., 5489 Arnqld, Walter, 5393 5678 5771 Simpson, Warren J., 5633 Asoh, Sadamitsu, 5692 Ganem, Don, McHenry, Charles S., 5735 Singer, R.
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    Distribution of Cytochromes in Bacteria: Relationship to General Physiology DAVID J

    INTERNATIONAL JOURNAL of SYSTEMATIC BACTERIOLOGY Vol. 23, No. 4 October 1973, p. 459-467 Prin ted in U.S.A. Copyright 0 1973 International Association of Microbiological Societies Distribution of Cytochromes in Bacteria: Relationship to General Physiology DAVID J. MEYER' and COLIN W. JONES Department of Biochemistry, The University of Leicester, England A review of cytochrome occurrence in bacteria is presented which gives the taxonomic distribution of cytochromes and which relates this to general physiological characteristics. Data obtained from published research and recent experimental studies on a total of 169 species of bacteria suggested the existence of four major groupings: (i) the aerobic and facultatively anaerobic, heterotrophic gram positives (cytochrome pattern aa3.0. b.c); (ii) the aerobic and facultatively anaerobic, heterotrophic gram negatives (cytochrome pattern either al.d.o.b.c, a1.o.b.c or aa3.o.b.c); (iii) anaerobic and microaerophilic hetero- trophs (cytochrome pattern b sometimes with al /d/o), and (iv) the ch'emo- and photo-autotrophs (cytochrome pattern c plus czl /aa3/o/b). The absence or minor presence of cytochrome c in facultatively anaerobic and anaerobic heterotrophs was confirmed and was also observed in plant and animal pathogens. Cytochrome d was confined in occurrence mainly to a small taxonomic group of organisms characterized by a high degree of adaptability to unstable habitats. This group was considered for further subdivision dependent upon the conditions causing the production of cytochrome d. As part of an investigation into the occur- ilated on organisms in the three major bacterial orders: rence of more than one spectral type of (i) the taxonomic status of the species according to cytochrome oxidase in many bacteria, a survey Bergey 's Manual of Determinative Bacteriology (13) of published data was carried out.
  • Current Understanding on Cytochrome Bd Quinol Oxidase of Escherichia Coli a Mutagenesis, Kinetics and Spectroscopic Study by Ke

    Current Understanding on Cytochrome Bd Quinol Oxidase of Escherichia Coli a Mutagenesis, Kinetics and Spectroscopic Study by Ke

    CURRENT UNDERSTANDING ON CYTOCHROME BD QUINOL OXIDASE OF ESCHERICHIA COLI A MUTAGENESIS, KINETICS AND SPECTROSCOPIC STUDY BY KE YANG DISSERTATION Submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biochemistry in the Graduate College of the University of Illinois at Urbana-Champaign, 2009 Urbana, Illinois Doctoral Committee: Professor Robert B. Gennis, Chair Professor Robert B. Gennis, Director of Research Professor Deborah E. Leckband Associate Professor Satish K. Nair Assistant Professor Maria Spies ABSTRACT Time-resolved kinetics study on the cytochrome bd quinol oxidase from Escherichia coli was carried out by stopped-flow techniques. The natural substrate, ubiquinol, was used to turnover the enzyme in the fast catalysis successfully for the first time. The results excluded the fully oxidized form of the enzyme from the rapid catalytic cycle of cytochrome bd oxidase. A re-investigation by both Flow-Flash and EPR on the previously reported mutant at Glu445 in subunit I, uncovered the dithionite-resistant ferric heme b595. Electrometrics data further suggested a series of protonatable groups forming a proton channel located in the membrane to facilitate the proton translocation from cytoplasm to the heme b595 / heme d binuclear center. With help of the increasing database of available cytochrome bd oxidase sequences, site-directed mutagenesis studies were carried out on the highly conserved residues of the enzyme. Mutations on two highly conserved acidic residues in subunit I – Glu99 and Glu107 were characterized in detail. The glutamine substitution at Glu107 was managed to obtain the FTIR redox difference spectra regarding its relatively intact binuclear center. Glu107 was shown to be protonated at pH 7.6 and that it was perturbed by the reduction of the heme b595 / heme d binuclear center at the active site.