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Gene Review

VIA L  -  cytochrome-c oxidase

Bos taurus

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Disease relevance of VIA L


Psychiatry related information on VIA L


High impact information on VIA L

  • Cell respiration in mitochondria and some bacteria is catalysed by cytochrome c oxidase, which reduces O2 to water, coupled with translocation of four protons across the mitochondrial or bacterial membrane [6].
  • Crystal structures of bovine heart cytochrome c oxidase in the fully oxidized, fully reduced, azide-bound, and carbon monoxide-bound states were determined at 2.30, 2.35, 2.9, and 2.8 angstrom resolution, respectively [7].
  • All 13 lipids, including two cardiolipins, one phosphatidylcholine, three phosphatidylethanolamines, four phosphatidylglycerols and three triglycerides, were identified in a crystalline bovine heart cytochrome c oxidase (CcO) preparation [8].
  • We show that all cytochrome c oxidase (complex IV) of Saccharomyces cerevisiae is bound to cytochrome c reductase (complex III), which exists in three forms: the free dimer, and two supercomplexes comprising an additional one or two complex IV monomers [9].
  • By antibody screening of a rat liver and a rat heart cDNA library in lambda gt11 two clones coding for the liver- and heart-specific subunit VIa of rat cytochrome c oxidase were isolated [10].

Chemical compound and disease context of VIA L


Biological context of VIA L


Anatomical context of VIA L


Associations of VIA L with chemical compounds


Enzymatic interactions of VIA L

  • Attempts to rationalize the kinetics of cytochrome c oxidation catalyzed by solubilized mitochondrial cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC have been based on assumptions of productive complex formation (Michaelis-Menten approach) [28].

Regulatory relationships of VIA L


Other interactions of VIA L


Analytical, diagnostic and therapeutic context of VIA L


  1. The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer. Konstantinov, A.A., Siletsky, S., Mitchell, D., Kaulen, A., Gennis, R.B. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  2. Mössbauer study of a bacterial cytochrome oxidase: cytochrome c1aa3 from Thermus thermophilus. Kent, T.A., Münck, E., Dunham, W.R., Filter, W.F., Findling, K.L., Yoshida, T., Fee, J.A. J. Biol. Chem. (1982) [Pubmed]
  3. Functional reconstitution of membrane proteins in monolayer liposomes from bipolar lipids of Sulfolobus acidocaldarius. Elferink, M.G., de Wit, J.G., Demel, R., Driessen, A.J., Konings, W.N. J. Biol. Chem. (1992) [Pubmed]
  4. Electrostatic study of the proton pumping mechanism in bovine heart cytochrome C oxidase. Popović, D.M., Stuchebrukhov, A.A. J. Am. Chem. Soc. (2004) [Pubmed]
  5. Protein and lipid structural transitions in cytochrome c oxidase-dimyristoylphosphatidylcholine reconstitutions. Rigell, C.W., de Saussure, C., Freire, E. Biochemistry (1985) [Pubmed]
  6. Proton translocation by cytochrome c oxidase. Verkhovsky, M.I., Jasaitis, A., Verkhovskaya, M.L., Morgan, J.E., Wikström, M. Nature (1999) [Pubmed]
  7. Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase. Yoshikawa, S., Shinzawa-Itoh, K., Nakashima, R., Yaono, R., Yamashita, E., Inoue, N., Yao, M., Fei, M.J., Libeu, C.P., Mizushima, T., Yamaguchi, H., Tomizaki, T., Tsukihara, T. Science (1998) [Pubmed]
  8. Structures and physiological roles of 13 integral lipids of bovine heart cytochrome c oxidase. Shinzawa-Itoh, K., Aoyama, H., Muramoto, K., Terada, H., Kurauchi, T., Tadehara, Y., Yamasaki, A., Sugimura, T., Kurono, S., Tsujimoto, K., Mizushima, T., Yamashita, E., Tsukihara, T., Yoshikawa, S. EMBO J. (2007) [Pubmed]
  9. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. Schägger, H., Pfeiffer, K. EMBO J. (2000) [Pubmed]
  10. Characterization of two different genes (cDNA) for cytochrome c oxidase subunit VIa from heart and liver of the rat. Schlerf, A., Droste, M., Winter, M., Kadenbach, B. EMBO J. (1988) [Pubmed]
  11. C-terminal truncation and histidine-tagging of cytochrome c oxidase subunit II reveals the native processing site, shows involvement of the C-terminus in cytochrome c binding, and improves the assay for proton pumping. Hiser, C., Mills, D.A., Schall, M., Ferguson-Miller, S. Biochemistry (2001) [Pubmed]
  12. Control of respiration by nitric oxide in Keilin-Hartree particles, mitochondria and SH-SY5Y neuroblastoma cells. Mastronicola, D., Genova, M.L., Arese, M., Barone, M.C., Giuffrè, A., Bianchi, C., Brunori, M., Lenaz, G., Sarti, P. Cell. Mol. Life Sci. (2003) [Pubmed]
  13. Water-hydroxide exchange reactions at the catalytic site of heme-copper oxidases. Brändén, M., Namslauer, A., Hansson, O., Aasa, R., Brzezinski, P. Biochemistry (2003) [Pubmed]
  14. Multifrequency EPR evidence for a bimetallic center at the CuA site in cytochrome c oxidase. Kroneck, P.M., Antholine, W.E., Kastrau, D.H., Buse, G., Steffens, G.C., Zumft, W.G. FEBS Lett. (1990) [Pubmed]
  15. Electrophoretically monodisperse cytochrome c oxidases. Heinrichs, M., Buse, G. Biochem. Biophys. Res. Commun. (1988) [Pubmed]
  16. Single catalytic site model for the oxidation of ferrocytochrome c by mitochondrial cytochrome c oxidase. Speck, S.H., Dye, D., Margoliash, E. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  17. Direct measurement of proton release by cytochrome c oxidase in solution during the F-->O transition. Zaslavsky, D., Sadoski, R.C., Rajagukguk, S., Geren, L., Millett, F., Durham, B., Gennis, R.B. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  18. Chronic exposure to nitric oxide alters the free iron pool in endothelial cells: role of mitochondrial respiratory complexes and heat shock proteins. Ramachandran, A., Ceaser, E., Darley-Usmar, V.M. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  19. Developmental regulation of tissue-specific isoforms of subunit VIa of beef cytochrome c oxidase. Schillace, R., Preiss, T., Lightowlers, R.N., Capaldi, R.A. Biochim. Biophys. Acta (1994) [Pubmed]
  20. Crystallization of part of the mitochondrial electron transfer chain: cytochrome c oxidase--cytochrome c complex. Ozawa, T., Suzuki, H., Tanaka, M. Proc. Natl. Acad. Sci. U.S.A. (1980) [Pubmed]
  21. Incorporation of beef heart cytochrome c oxidase as a proton-motive force-generating mechanism in bacterial membrane vesicles. Driessen, A.J., de Vrij, W., Konings, W.N. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  22. Crystalline cytochrome c oxidase of bovine heart mitochondrial membrane: composition and x-ray diffraction studies. Yoshikawa, S., Tera, T., Takahashi, Y., Tsukihara, T., Caughey, W.S. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  23. Arrangement of the subunits in solubilized and membrane-bound cytochrome c oxidase from bovine heart. Eytan, G.D., Carroll, R.C., Schatz, G., Racker, E. J. Biol. Chem. (1975) [Pubmed]
  24. Diphosphatidylglycerol is required for optimal activity of beef heart cytochrome c oxidase. Vik, S.B., Georgevich, G., Capaldi, R.A. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  25. Nitric oxide inhibition of respiration involves both competitive (heme) and noncompetitive (copper) binding to cytochrome c oxidase. Mason, M.G., Nicholls, P., Wilson, M.T., Cooper, C.E. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  26. Resolution of the electronic transitions of cytochrome c oxidase: evidence for two conformational states of ferrous cytochrome alpha. Sherman, D., Kotake, S., Ishibe, N., Copeland, R.A. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  27. Affinity chromatography purification of cytochrome c binding enzymes. Azzi, A., Bill, K., Broger, C. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  28. Oxidation of ferrocytochrome c by mitochondrial cytochrome c oxidase. Errede, B., Haight, G.P., Kamen, M.D. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
  29. The cytochrome c oxidase-cytochrome c complex: spectroscopic analysis of conformational changes in the protein-protein interaction domain. Michel, B., Proudfoot, A.E., Wallace, C.J., Bosshard, H.R. Biochemistry (1989) [Pubmed]
  30. Cloning and sequencing of the cDNA for a 13th different subunit (IHQ) of beef heart cytochrome c oxidase. Lightowlers, R., Takamiya, S., Wessling, R., Lindorfer, M., Capaldi, R.A. J. Biol. Chem. (1989) [Pubmed]
  31. Studies on cytochrome c oxidase, X. Isolation and amino-acid sequence of polypeptide VIIIb. Meinecke, L., Steffens, G.J., Buse, G. Hoppe-Seyler's Z. Physiol. Chem. (1984) [Pubmed]
  32. Studies on cytochrome c oxidase, XII. Isolation and primary structure of polypeptide VIb from bovine heart. Meinecke, L., Buse, G. Biol. Chem. Hoppe-Seyler (1985) [Pubmed]
  33. Anesthetic-like interactions of nitric oxide with albumin and hemeproteins. A mechanism for control of protein function. Sampath, V., Zhao, X.J., Caughey, W.S. J. Biol. Chem. (2001) [Pubmed]
  34. Spectroscopic characterization of compound C and related derivatives of cytochrome oxidase. Carter, K.R., Antalis, T.M., Palmer, G., Ferris, N.S., Woodruff, W.H. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  35. The catalytic cycle of cytochrome c oxidase is not the sum of its two halves. Bloch, D., Belevich, I., Jasaitis, A., Ribacka, C., Puustinen, A., Verkhovsky, M.I., Wikström, M. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  36. Cytochrome c oxidase. Ostermeier, C., Iwata, S., Michel, H. Curr. Opin. Struct. Biol. (1996) [Pubmed]
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