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Gene Review

CYC1  -  cytochrome c-1

Bos taurus

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Disease relevance of CYC1

  • The nucleotide sequence coding for bovine leukemia virus (BLV) envelope glycoprotein gp51 was inserted into a yeast-Escherichia coli shuttle vector carrying the promoter and secretion signal sequence of PHO5 (the yeast gene coding for repressible acid phosphatase) and the CYC1 transcriptional terminator [1].
  • The interaction domain for cytochrome c on the cytochrome bc(1) complex was studied using a series of Rhodobacter sphaeroides cytochrome bc(1) mutants in which acidic residues on the surface of cytochrome c(1) were substituted with neutral or basic residues [2].
  • Exposure to DETA-NO resulted in a decrease in Psim and concomitant release of cytochrome c and caspase-9 activation, which were enhanced by hypoxia [3].
  • Anabaena Fld residues Asp144 and Glu145 align closely with rat P450 reductase residue Asp208, which has been shown by mutagenesis to be important in electron transfer to P4502B1 but not to cytochrome c (Shen, A. L., and Kasper, C. B. (1995) J. Biol. Chem. 270, 27475-27480) [4].
  • Rhizobium phaseoli cytochrome c-deficient mutant induces empty nodules on Phaseolus vulgaris L [5].

High impact information on CYC1

  • The enzyme's catalytic cycle consists of a reductive phase, in which the oxidized enzyme receives electrons from cytochrome c, and an oxidative phase, in which the reduced enzyme is oxidized by O2 [6].
  • On the basis of x-ray diffraction data to a resolution of 2.9 angstroms, atomic models of most protein components of the bovine cytochrome bc1 complex were built, including core 1, core 2, cytochrome b, subunit 6, subunit 7, a carboxyl-terminal fragment of cytochrome c1, and an amino-terminal fragment of the iron-sulfur protein [7].
  • Lymphocyte specificity to protein antigens. II. Fine specificity of T-cell activation with cytochrome c and derived peptides as antigenic probes [8].
  • The pattern of specificity observed appeared to be haplotype (BDF1) dependent although similar conclusions about the fine specificity of T cells in the response to cytochrome c have been obtained in other strains but associated with different residues [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].

Chemical compound and disease context of CYC1

  • Respiration during hypoxia was also inhibited when N,N,N',N'-tetramethyl-p-phenylenediamine (0.5 mM) and ascorbate (5 mM) were used to reduce cytochrome c, suggesting that cytochrome oxidase was partially inhibited [10].
  • In addition, we describe the results of calculations of C(alpha), C(beta), C(gamma)1, C(gamma)2, and C(delta) shifts in the two isoleucine residues in bovine pancreatic trypsin inhibitor and the four isoleucines in a cytochrome c and demonstrate that the side chain chemical shifts are strongly influenced by chi(2) torsion angle effects [11].
  • Photolabelling with 8-azido-ATP of the reconstituted Paracoccus enzyme also increases the Km for cytochrome c which is completely prevented if ATP but not if ADP is present during illumination as was found with reconstituted cytochrome c oxidase from bovine heart [12].
  • Following incubation with increasing amounts of DCCD, proton ejection was recorded in response to reductant pulses with reduced cytochrome c. Concentrations of DCCD which greatly reduced proton pumping by bovine cytochrome c oxidase used as a control were found to exert only a minor effect on proton translocation by Paracoccus oxidase [13].
  • All nitroalkane oxidations by these three flavoenzymes are inhibited by Cu and Zn-superoxide dismutase of bovine blood, Mn-superoxide dismutases of bacilli, Fe-superoxide dismutase of Serratia marcescens, and other O2-. scavengers such as cytochrome c and NADH, but are not affected by hydroxyl radical scavengers such as mannitol [14].

Biological context of CYC1


Anatomical context of CYC1

  • Effect of cytochrome c on the generation and elimination of O2*- and H2O2 in mitochondria [15].
  • The presence of a hydrophobic cluster near the COOH-terminal region indicates that the COOH-terminal region of cytochrome C1 associates with, or is buried in, the phospholipid bilayer of the mitochondrial membrane [19].
  • The O(2)(*) and H(2)O(2) generation in cytochrome c-depleted Keilin-Hartree heart muscle preparation (HMP) is 7-8 times higher than that in normal HMP [15].
  • Cytochrome oxidase (ferrocytochrome c:oxygen oxidoreductase, EC of beef heart mitochondria, prepared by a standard method and brought to the highest purity level, is essentially inactive when tested in the aerobic assay involving oxidation of reduced cytochrome c by molecular oxygen [20].
  • Bovine aortic endothelial cells were treated with chloramphenicol, which resulted in a decreased ratio of mitochondrial complex IV to cytochrome c and increased oxidant production in the cell [21].

Associations of CYC1 with chemical compounds


Physical interactions of CYC1


Enzymatic interactions of CYC1


Regulatory relationships of CYC1


Other interactions of CYC1

  • No clear homology was found between cytochrome c1 and other membranous proteins such as cytochrome b5 or the subunits of cytochrome oxidase for which sequences have been reported [19].
  • While the reduction of cytochrome c, reflecting the interaction between adrenodoxin and its reductase, and the interaction with CYP11B1 have not been significantly affected by the presence of the presequence, the binding affinity of preadrenodoxin to CYP11A1 is 5.5-fold lower than that of the mature form [34].
  • We verified that purified cytochrome b561 can donate electron equivalents directly to cytochrome c. The purified cytochrome b561 was successfully reconstituted into cholesterol-phosphatidylcholine-phosphatidylglycerol vesicles by a detergent-dialysis and extrusion method [29].
  • Treatment of adrenodoxin reductase with a highly purified preparation of neuraminidase demonstrates that neither the adrenodoxin-independent ferricyanide reductase activity nor the adrenodoxin-dependent cytochrome c reductase activity of the enzyme is affected by neuraminidase treatment [35].
  • Our results suggest that FABP scavenges O2-, OH. and OCl. as indicated by the FABP inhibition of O2- -dependent reduction of cytochrome c, OH.-dependent hydroxybenzoic acid formation and OCl.-mediated chemiluminescence response [36].

Analytical, diagnostic and therapeutic context of CYC1


  1. Biochemical and immunological characterization of the bovine leukemia virus (BLV) envelope glycoprotein (gp51) produced in Saccharomyces cerevisiae. Legrain, M., Portetelle, D., Dumont, J., Burny, A., Hilger, F. Gene (1989) [Pubmed]
  2. Definition of the interaction domain for cytochrome c on the cytochrome bc(1) complex. Steady-state and rapid kinetic analysis of electron transfer between cytochrome c and Rhodobacter sphaeroides cytochrome bc(1) surface mutants. Tian, H., Sadoski, R., Zhang, L., Yu, C.A., Yu, L., Durham, B., Millett, F. J. Biol. Chem. (2000) [Pubmed]
  3. Hypoxia potentiates nitric oxide-mediated apoptosis in endothelial cells via peroxynitrite-induced activation of mitochondria-dependent and -independent pathways. Walford, G.A., Moussignac, R.L., Scribner, A.W., Loscalzo, J., Leopold, J.A. J. Biol. Chem. (2004) [Pubmed]
  4. Negatively charged anabaena flavodoxin residues (Asp144 and Glu145) are important for reconstitution of cytochrome P450 17alpha-hydroxylase activity. Jenkins, C.M., Genzor, C.G., Fillat, M.F., Waterman, M.R., Gómez-Moreno, C. J. Biol. Chem. (1997) [Pubmed]
  5. Rhizobium phaseoli cytochrome c-deficient mutant induces empty nodules on Phaseolus vulgaris L. Soberón, M., Aguilar, G.R., Sánchez, F. Mol. Microbiol. (1993) [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. Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria. Xia, D., Yu, C.A., Kim, H., Xia, J.Z., Kachurin, A.M., Zhang, L., Yu, L., Deisenhofer, J. Science (1997) [Pubmed]
  8. Lymphocyte specificity to protein antigens. II. Fine specificity of T-cell activation with cytochrome c and derived peptides as antigenic probes. Corradin, G., Chiller, J.M. J. Exp. Med. (1979) [Pubmed]
  9. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. Schägger, H., Pfeiffer, K. EMBO J. (2000) [Pubmed]
  10. Cellular respiration during hypoxia. Role of cytochrome oxidase as the oxygen sensor in hepatocytes. Chandel, N.S., Budinger, G.R., Choe, S.H., Schumacker, P.T. J. Biol. Chem. (1997) [Pubmed]
  11. Carbon-13 NMR shielding in the twenty common amino acids: comparisons with experimental results in proteins. Sun, H., Sanders, L.K., Oldfield, E. J. Am. Chem. Soc. (2002) [Pubmed]
  12. Intraliposomal nucleotides change the kinetics of reconstituted cytochrome c oxidase from bovine heart but not from Paracoccus denitrificans. Hüther, F.J., Kadenbach, B. Biochem. Biophys. Res. Commun. (1988) [Pubmed]
  13. Dicyclohexylcarbodiimide does not inhibit proton pumping by cytochrome c oxidase of Paracoccus denitrificans. Püttner, I., Solioz, M., Carafoli, E., Ludwig, B. Eur. J. Biochem. (1983) [Pubmed]
  14. Oxidation of anionic nitroalkanes by flavoenzymes, and participation of superoxide anion in the catalysis. Kido, T., Soda, K. Arch. Biochem. Biophys. (1984) [Pubmed]
  15. Effect of cytochrome c on the generation and elimination of O2*- and H2O2 in mitochondria. Zhao, Y., Wang, Z.B., Xu, J.X. J. Biol. Chem. (2003) [Pubmed]
  16. High yield synthesis of the bovine leukemia virus (BLV) p24 major internal protein in Saccharomyces cerevisiae. Dumont, J., Legrain, M., Portetelle, D., Brasseur, R., Burny, A., Hilger, F. Gene (1989) [Pubmed]
  17. Definition of cytochrome c binding domains by chemical modification: kinetics of reaction with beef mitochondrial reductase and functional organization of the respiratory chain. Speck, S.H., Ferguson-Miller, S., Osheroff, N., Margoliash, E. Proc. Natl. Acad. Sci. U.S.A. (1979) [Pubmed]
  18. 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]
  19. Structural studies of bovine heart cytochrome c1. Wakabayashi, S., Matsubara, H., Kim, C.H., King, T.E. J. Biol. Chem. (1982) [Pubmed]
  20. On reagents that convert cytochrome oxidase from an inactive to an active coupling state. Green, D.E., Fry, M. Proc. Natl. Acad. Sci. U.S.A. (1980) [Pubmed]
  21. Inhibition of mitochondrial protein synthesis results in increased endothelial cell susceptibility to nitric oxide-induced apoptosis. Ramachandran, A., Moellering, D.R., Ceaser, E., Shiva, S., Xu, J., Darley-Usmar, V. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  22. Crystallization of cytochrome bc1 complex. Ozawa, T., Tanaka, M., Shimomura, Y. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  23. Crystallization of the middle part of the mitochondrial electron transfer chain: cytochrome bc1-cytochrome c complex. Ozawa, T., Tanaka, M., Shimomura, Y. Proc. Natl. Acad. Sci. U.S.A. (1980) [Pubmed]
  24. Anti-immunoglobulin augments the B-cell antigen-presentation function independently of internalization of receptor-antigen complex. Casten, L.A., Lakey, E.K., Jelachich, M.L., Margoliash, E., Pierce, S.K. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  25. C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450. Uhlmann, H., Kraft, R., Bernhardt, R. J. Biol. Chem. (1994) [Pubmed]
  26. 13C NMR spectroscopic and X-ray crystallographic study of the role played by mitochondrial cytochrome b5 heme propionates in the electrostatic binding to cytochrome c. Rodríguez-Marañón, M.J., Qiu, F., Stark, R.E., White, S.P., Zhang, X., Foundling, S.I., Rodríguez, V., Schilling, C.L., Bunce, R.A., Rivera, M. Biochemistry (1996) [Pubmed]
  27. 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]
  28. 3-Methoxybenzidine: a potent inhibitor of cholesterol side chain cleavage cytochrome P-450. Duval, J.F., Vickery, L.E. Steroids (1980) [Pubmed]
  29. Reversely-oriented cytochrome b561 in reconstituted vesicles catalyzes transmembrane electron transfer and supports extravesicular dopamine beta-hydroxylase activity. Seike, Y., Takeuchi, F., Tsubaki, M. J. Biochem. (2003) [Pubmed]
  30. Spatial organization of redox active centers in the bovine heart ubiquinol-cytochrome c oxidoreductase. Ohnishi, T., Schägger, H., Meinhardt, S.W., LoBrutto, R., Link, T.A., von Jagow, G. J. Biol. Chem. (1989) [Pubmed]
  31. 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]
  32. Tumor necrosis factor-alpha and lipopolysaccharide induce apoptotic cell death in bovine glomerular endothelial cells. Messmer, U.K., Briner, V.A., Pfeilschifter, J. Kidney Int. (1999) [Pubmed]
  33. Cocaine-mediated apoptosis in bovine coronary artery endothelial cells: role of nitric oxide. He, J., Xiao, Y., Zhang, L. J. Pharmacol. Exp. Ther. (2001) [Pubmed]
  34. Impact of the presequence of a mitochondrium-targeted precursor, preadrenodoxin, on folding, catalytic activity, and stability of the protein in vitro. Goder, V., Beckert, V., Pfeil, W., Bernhardt, R. Arch. Biochem. Biophys. (1998) [Pubmed]
  35. Structural and functional characterization of bovine adrenodoxin reductase by limited proteolysis. Warburton, R.J., Seybert, D.W. Biochim. Biophys. Acta (1995) [Pubmed]
  36. Free radical scavenging by myocardial fatty acid binding protein. Samanta, A., Das, D.K., Jones, R., George, A., Prasad, M.R. Free Radic. Res. Commun. (1989) [Pubmed]
  37. Affinity chromatography purification of cytochrome c binding enzymes. Azzi, A., Bill, K., Broger, C. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  38. 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]
  39. Platelet-activating factor may act as a second messenger in the release of icosanoids and superoxide anions from leukocytes and endothelial cells. Stewart, A.G., Dubbin, P.N., Harris, T., Dusting, G.J. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  40. The presence of a reducible disulfide bond in milk xanthine oxidase. Hille, R., Massey, V. J. Biol. Chem. (1982) [Pubmed]
  41. Purification and characterization of tetrahydrofolate.protein complex in bovine liver. Watabe, S. J. Biol. Chem. (1978) [Pubmed]
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