cyoD

Summary

Gene Symbol: cyoD
Description: cytochrome o ubiquinol oxidase subunit IV
Alias: ECK0423, JW0419
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Saiki K, Nakamura H, Mogi T, Anraku Y. Probing a role of subunit IV of the Escherichia coli bo-type ubiquinol oxidase by deletion and cross-linking analyses. J Biol Chem. 1996;271:15336-40 pubmed
    Subunit IV of the Escherichia coli bo-type ubiquinol oxidase is a 12-kDa membrane protein encoded by the cyoD gene and is conserved in the bacterial heme-copper terminal oxidases...
  2. Kita K, Kasahara M, Anraku Y. Formation of a membrane potential by reconstructed liposomes made with cytochrome b562-o complex, a terminal oxidase of Escherichia coli K12. J Biol Chem. 1982;257:7933-5 pubmed
    ..This is the first indication that there is a coupling site in an E. coli terminal oxidase, which consists of b-type cytochromes. ..
  3. Nakamura H, Yamato I, Anraku Y, Lemieux L, Gennis R. Expression of cyoA and cyoB demonstrates that the CO-binding heme component of the Escherichia coli cytochrome o complex is in subunit I. J Biol Chem. 1990;265:11193-7 pubmed
    ..This heme component is shown to bind to CO, as it does in the intact enzyme. Hence, subunit I alone is sufficient for the assembly of the stable CO-binding heme component of this oxidase. ..
  4. Saraste M, Raitio M, Jalli T, Chepuri V, Lemieux L, Gennis R. Cytochrome o from Escherichia coli is structurally related to cytochrome aa3. Ann N Y Acad Sci. 1988;550:314-24 pubmed
  5. Garcia Horsman J, Barquera B, Rumbley J, Ma J, Gennis R. The superfamily of heme-copper respiratory oxidases. J Bacteriol. 1994;176:5587-600 pubmed
  6. Yap L, Samoilova R, Gennis R, Dikanov S. Characterization of the exchangeable protons in the immediate vicinity of the semiquinone radical at the QH site of the cytochrome bo3 from Escherichia coli. J Biol Chem. 2006;281:16879-87 pubmed
    ..The results support a model that the semiquinone is bound to the protein in a very asymmetric manner by two strong hydrogen bonds from Asp-75 and Arg-71 to the O1 carbonyl, while the O4 carbonyl is not hydrogen-bonded to the protein. ..
  7. Musser S, Stowell M, Lee H, Rumbley J, Chan S. Uncompetitive substrate inhibition and noncompetitive inhibition by 5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole (UHDBT) and 2-n-nonyl-4-hydroxyquinoline-N-oxide (NQNO) is observed for the cytochrome bo3 complex: implications for a Q(H2)-loop proton . Biochemistry. 1997;36:894-902 pubmed
  8. Cheesman M, Oganesyan V, Watmough N, Butler C, Thomson A. The nature of the exchange coupling between high-spin Fe(III) heme o3 and CuBII in Escherichia coli quinol oxidase, cytochrome bo3: MCD and EPR studies. J Am Chem Soc. 2004;126:4157-66 pubmed
    ..These conclusions overturn a long-held view that such EPR signals in bovine cytochrome c oxidase arise from an S' = 2 ground state resulting from strong exchange coupling (J > 10(2) cm-1) within the active site. ..
  9. Morgan J, Verkhovsky M, Puustinen A, Wikstrom M. Identification of a "peroxy" intermediate in cytochrome bo3 of Escherichia coli. Biochemistry. 1995;34:15633-7 pubmed
    ..This intermediate subsequently relaxes into the "ferryl" species which has been described previously. We conclude that the oxygen reaction is similar in the cytochrome c and quinol oxidases. ..

More Information

Publications46

  1. Minghetti K, Goswitz V, Gabriel N, Hill J, Barassi C, Georgiou C, et al. Modified, large-scale purification of the cytochrome o complex (bo-type oxidase) of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity. Biochemistry. 1992;31:6917-24 pubmed
    ..Hence, although subunit II does not contain CuA and does not interact with cytochrome c, it still must have an important function in the bo-type ubiquinol oxidase. ..
  2. Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson Ek M, Laakkonen L, et al. The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. Nat Struct Biol. 2000;7:910-7 pubmed publisher
    ..In light of these findings we suggest specific roles for these polar residues in electron and proton transfer in ubiquinol oxidase...
  3. Matsushita K, Patel L, Gennis R, Kaback H. Reconstitution of active transport in proteoliposomes containing cytochrome o oxidase and lac carrier protein purified from Escherichia coli. Proc Natl Acad Sci U S A. 1983;80:4889-93 pubmed
    ..The results provide powerful additional support for the "chemiosmotic hypothesis" and demonstrate that purified lac carrier protein retains the ability to function in a physiological manner. ..
  4. Puustinen A, Finel M, Virkki M, Wikstrom M. Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli. FEBS Lett. 1989;249:163-7 pubmed
    ..coli from which cytochrome d was deleted. These observations show that the cytochrome o complex is a proton pump much like cytochrome aa3 to which it is structurally related. ..
  5. Iuchi S, Chepuri V, Fu H, Gennis R, Lin E. Requirement for terminal cytochromes in generation of the aerobic signal for the arc regulatory system in Escherichia coli: study utilizing deletions and lac fusions of cyo and cyd. J Bacteriol. 1990;172:6020-5 pubmed
  6. Jeuken L, Connell S, Henderson P, Gennis R, Evans S, Bushby R. Redox enzymes in tethered membranes. J Am Chem Soc. 2006;128:1711-6 pubmed
    ..Enzyme coverages observed with TM-AFM and CV coincide (2-8.5 fmol.cm(-)(2)), indicating that most-if not all-cbo(3) on the surface is catalytically active and thus retains its integrity during immobilization. ..
  7. Frericks H, Zhou D, Yap L, Gennis R, Rienstra C. Magic-angle spinning solid-state NMR of a 144 kDa membrane protein complex: E. coli cytochrome bo3 oxidase. J Biomol NMR. 2006;36:55-71 pubmed
  8. Nakamura H, Saiki K, Mogi T, Anraku Y. Assignment and functional roles of the cyoABCDE gene products required for the Escherichia coli bo-type quinol oxidase. J Biochem. 1997;122:415-21 pubmed
    ..Present findings suggest that subunits II, III, and IV of the oxidase complex are required for the assembly of the metal centers in subunit I. ..
  9. Uchida T, Mogi T, Nakamura H, Kitagawa T. Role of Tyr-288 at the dioxygen reduction site of cytochrome bo studied by stable isotope labeling and resonance raman spectroscopy. J Biol Chem. 2004;279:53613-20 pubmed
    ..Our results suggested that the substitution of ring hydrogens of Tyr-288 with deuteriums slows down the formation of the His-Tyr cross-link essential for dioxygen reduction at the binuclear center. ..
  10. Au D, Lorence R, Gennis R. Isolation and characterization of an Escherichia coli mutant lacking the cytochrome o terminal oxidase. J Bacteriol. 1985;161:123-7 pubmed
    ..Introduction of the cyd+ allele into the strain restores the respiration function of the strain, indicating that the cytochrome o branch of the respiratory chain is dispensable under normal laboratory growth conditions. ..
  11. Puustinen A, Finel M, Haltia T, Gennis R, Wikstrom M. Properties of the two terminal oxidases of Escherichia coli. Biochemistry. 1991;30:3936-42 pubmed
    ..3-0.7. This was attributed to an "inside out" orientation of a significant fraction of the enzyme. Possible metabolic benefits of expressing both cytochromes bo and d in E. coli are discussed. ..
  12. Lorence R, Carter K, Green G, Gennis R. Cytochrome b558 monitors the steady state redox state of the ubiquinone pool in the aerobic respiratory chain of Escherichia coli. J Biol Chem. 1987;262:10532-6 pubmed
    ..coli membranes, demonstrating that the rate-limiting step in the E. coli respiratory chain is at the dehydrogenases which feed electrons into the system. ..
  13. Cotter P, Darie S, Gunsalus R. The effect of iron limitation on expression of the aerobic and anaerobic electron transport pathway genes in Escherichia coli. FEMS Microbiol Lett. 1992;100:227-32 pubmed
    ..The above findings suggest that in addition to Fur, some other cellular protein may bind iron for reporting and regulating iron-dependent cell functions. ..
  14. Minagawa J, Mogi T, Gennis R, Anraku Y. Identification of heme and copper ligands in subunit I of the cytochrome bo complex in Escherichia coli. J Biol Chem. 1992;267:2096-104 pubmed
    ..We present a helical wheel model of the redox center in subunit I, which consists of the membrane-spanning regions II, VI, VII, and X, and discuss the implications of the model...
  15. Lemieux L, Calhoun M, Thomas J, Ingledew W, Gennis R. Determination of the ligands of the low spin heme of the cytochrome o ubiquinol oxidase complex using site-directed mutagenesis. J Biol Chem. 1992;267:2105-13 pubmed
  16. Ma J, Katsonouri A, Gennis R. Subunit II of the cytochrome bo3 ubiquinol oxidase from Escherichia coli is a lipoprotein. Biochemistry. 1997;36:11298-303 pubmed
    ..Hence, this unusual processing of a cytoplasmic membrane protein, which is already anchored to the membrane by two transmembrane helices, is not essential for either assembly or function. ..
  17. Tseng C, Albrecht J, Gunsalus R. Effect of microaerophilic cell growth conditions on expression of the aerobic (cyoABCDE and cydAB) and anaerobic (narGHJI, frdABCD, and dmsABC) respiratory pathway genes in Escherichia coli. J Bacteriol. 1996;178:1094-8 pubmed
    ..These two transcriptional regulators coordinate the hierarchial control of respiratory pathway gene expression in E. coli to ensure the optimal use of oxygen in the cell environment. ..
  18. Stenberg F, von Heijne G, Daley D. Assembly of the cytochrome bo3 complex. J Mol Biol. 2007;371:765-73 pubmed
    ..We also show that cofactor insertion catalyses assembly. These findings provide novel insights into the biogenesis of this model membrane protein complex. ..
  19. Chepuri V, Lemieux L, Hill J, Alben J, Gennis R. Recent studies of the cytochrome o terminal oxidase complex of Escherichia coli. Biochim Biophys Acta. 1990;1018:124-7 pubmed
    ..Site-directed mutagenesis is being utilized to define which amino acids are ligands to the heme iron and copper prosthetic groups. ..
  20. Jeuken L, Weiss S, Henderson P, Evans S, Bushby R. Impedance spectroscopy of bacterial membranes: coenzyme-Q diffusion in a finite diffusion layer. Anal Chem. 2008;80:9084-90 pubmed publisher
    ..It is hypothesized that this result represent perpendicular diffusion of quinone across the membrane, corresponding to a "flip" time between 0.05 and 1 s. ..
  21. Yang K, Borisov V, Konstantinov A, Gennis R. The fully oxidized form of the cytochrome bd quinol oxidase from E. coli does not participate in the catalytic cycle: direct evidence from rapid kinetics studies. FEBS Lett. 2008;582:3705-9 pubmed publisher
    ..The data support models of the catalytic cycle which do not include the fully oxidized form of the enzyme as an intermediate. ..
  22. Cotter P, Gunsalus R. Contribution of the fnr and arcA gene products in coordinate regulation of cytochrome o and d oxidase (cyoABCDE and cydAB) genes in Escherichia coli. FEMS Microbiol Lett. 1992;70:31-6 pubmed
    ..coli. Additionally, the expression of the fnr regulatory gene, and regulation of the anaerobic respiratory genes, narGHJI, dmsABC and frdABCD, was found to be independent of ArcA. ..
  23. Peercy B, Cox S, Shalel Levanon S, San K, Bennett G. A kinetic model of oxygen regulation of cytochrome production in Escherichia coli. J Theor Biol. 2006;242:547-63 pubmed
    ..Toward this end we build and analyse a mathematical model that captures the role played by oxygen in the regulation of cytochrome production in E. coli. ..
  24. Chepuri V, Lemieux L, Au D, Gennis R. The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases. J Biol Chem. 1990;265:11185-92 pubmed
    ..coli oxidase and the aa3-type cytochrome c oxidases must have very similar structures, at least in the vicinity of the catalytic centers, and they are very likely to have similar mechanisms for bioenergetic coupling (proton pumping). ..
  25. Choi S, Lin M, Ouyang H, Gennis R. Searching for the low affinity ubiquinone binding site in cytochrome bo3 from Escherichia coli. Biochim Biophys Acta Bioenerg. 2017;1858:366-370 pubmed publisher
    ..In the current work, this was tested by site-directed mutagenesis. The results show that these residues are not important for catalytic function and do not define the QL substrate binding site. ..
  26. Calhoun M, Newton G, Gennis R. E. coli map. Physical map locations of genes encoding components of the aerobic respiratory chain of Escherichia coli. J Bacteriol. 1991;173:1569-70 pubmed
  27. Oden K, DeVeaux L, Vibat C, Cronan J, Gennis R. Genomic replacement in Escherichia coli K-12 using covalently closed circular plasmid DNA. Gene. 1990;96:29-36 pubmed
    ..It is reported that such mutants may be constructed without linearizing plasmid DNA, as described previously. ..
  28. Kita K, Konishi K, Anraku Y. Terminal oxidases of Escherichia coli aerobic respiratory chain. I. Purification and properties of cytochrome b562-o complex from cells in the early exponential phase of aerobic growth. J Biol Chem. 1984;259:3368-74 pubmed
    ..The oxidase activity of the cytochrome b562-o complex was inhibited by photoinactivation with rose bengal, suggesting that the inhibition by zinc ion results from modification of a histidine residue of cytochrome o. ..
  29. Matsushita K, Patel L, Kaback H. Cytochrome o type oxidase from Escherichia coli. Characterization of the enzyme and mechanism of electrochemical proton gradient generation. Biochemistry. 1984;23:4703-14 pubmed
    ..In other words, cytochrome o oxidase from Escherichia coli does not appear to catalyze vectorial proton translocation. ..
  30. Kita K, Konishi K, Anraku Y. Purification and properties of two terminal oxidase complexes of Escherichia coli aerobic respiratory chain. Methods Enzymol. 1986;126:94-113 pubmed
    ..Thus, E. coli cells can maintain efficient oxidative energy conservation over a wide range of oxygen pressures by simply changing the contents of the two terminal oxidases, each of which functions as a coupling site. ..
  31. Au D, Gennis R. Cloning of the cyo locus encoding the cytochrome o terminal oxidase complex of Escherichia coli. J Bacteriol. 1987;169:3237-42 pubmed
    ..The cloned genes will be valuable for studying the structure, function, and regulation of the cytochrome o terminal oxidase complex. ..
  32. Welter R, Gu L, Yu L, Yu C, Rumbley J, Gennis R. Identification of the ubiquinol-binding site in the cytochrome bo3-ubiquinol oxidase of Escherichia coli. J Biol Chem. 1994;269:28834-8 pubmed
    ..This suggests that the ubiquinol-binding site of the cytochrome bo3 complex is located at least partially on subunit II. ..
  33. Ching E, Gennis R, Larsen R. Kinetics of intramolecular electron transfer in cytochrome bo3 from Escherichia coli. Biophys J. 2003;84:2728-33 pubmed
  34. Cotter P, Chepuri V, Gennis R, Gunsalus R. Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH, and the fnr gene product. J Bacteriol. 1990;172:6333-8 pubmed
    ..We also examined cyoABCDE and cydAB expression in response to growth on alternative carbon compounds and to changes in the culture medium pH and osmolarity. ..
  35. Chepuri V, Gennis R. The use of gene fusions to determine the topology of all of the subunits of the cytochrome o terminal oxidase complex of Escherichia coli. J Biol Chem. 1990;265:12978-86 pubmed
  36. Minagawa J, Nakamura H, Yamato I, Mogi T, Anraku Y. Transcriptional regulation of the cytochrome b562-o complex in Escherichia coli. Gene expression and molecular characterization of the promoter. J Biol Chem. 1990;265:11198-203 pubmed
  37. Matsushita K, Kaback H. D-lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome o oxidase. Biochemistry. 1986;25:2321-7 pubmed
    ..e., the oxidase catalyzes the scalar release of 2 H+ from ubiquinol on the outer surface of the membrane.(ABSTRACT TRUNCATED AT 250 WORDS) ..