CCP1/YKR066C Literature Guide Help

Other names published for CCP1: YKR066C

CCP1 - Function/Process (32)

ReferenceOther Genes Addressed
Dicarlo CM, et al.  (2011) Reduction potential of yeast cytochrome c peroxidase and three distal histidine mutants: Dependence on pH. J Inorg Biochem 105(4):532-7
Pearl NM, et al.  (2008) Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome C peroxidase: evidence for a single, catalytically active, cytochrome C binding domain. Biochemistry 47(9):2766-75
Pearl NM, et al.  (2007) Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: mutations near the high-affinity cytochrome c binding site. Biochemistry 46(28):8263-72
Tatsuta T, et al.  (2007) m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria. EMBO J 26(2):325-35
Nakani S, et al.  (2006) Characterization of a covalently linked yeast cytochrome c-cytochrome c peroxidase complex: evidence for a single, catalytically active cytochrome c binding site on cytochrome c peroxidase. Biochemistry 45(32):9887-93
Seifert JL, et al.  (2005) Hopping in the electron-transfer photocycle of the 1:1 complex of Zn-cytochrome c peroxidase with cytochrome c. J Am Chem Soc 127(16):5750-1
Branco MR, et al.  (2004) Decrease of H2O2 plasma membrane permeability during adaptation to H2O2 in Saccharomyces cerevisiae. J Biol Chem 279(8):6501-6
Jacobson T, et al.  (2004) Azide binding to yeast cytochrome c peroxidase and horse metmyoglobin: comparative thermodynamic investigation using isothermal titration calorimetry. Arch Biochem Biophys 422(2):125-36
Barros MH, et al.  (2003) H(2)O(2) generation in Saccharomyces cerevisiae respiratory pet mutants: effect of cytochrome c. Free Radic Biol Med 35(2):179-88
Kwon M, et al.  (2003) Oxidative stresses elevate the expression of cytochrome c peroxidase in Saccharomyces cerevisiae. Biochim Biophys Acta 1623(1):1-5
Minard KI and McAlister-Henn L  (2001) Antioxidant function of cytosolic sources of NADPH in yeast. Free Radic Biol Med 31(6):832-43
Pfister TD, et al.  (2001) The role of redox-active amino acids on compound I stability, substrate oxidation, and protein cross-linking in yeast cytochrome C peroxidase. Biochemistry 40(49):14942-51
Pielak GJ and Wang X  (2001) Interactions between yeast iso-1-cytochrome c and its peroxidase. Biochemistry 40(2):422-8
Iffland A, et al.  (2000) Directed molecular evolution of cytochrome c peroxidase. Biochemistry 39(35):10790-8
Charizanis C, et al.  (1999) The mitochondrial cytochrome c peroxidase Ccp1 of Saccharomyces cerevisiae is involved in conveying an oxidative stress signal to the transcription factor Pos9 (Skn7). Mol Gen Genet 262(3):437-47
Kanaya S, et al.  (1999) Studies of codon usage and tRNA genes of 18 unicellular organisms and quantification of Bacillus subtilis tRNAs: gene expression level and species-specific diversity of codon usage based on multivariate analysis. Gene 238(1):143-55
Palamakumbura AH, et al.  (1999) Oxidation of cytochrome c peroxidase to compound I by peroxyacids: evidence for rate-limiting diffusion through the protein matrix. Biochemistry 38(47):15647-52
Palamakumbura AH, et al.  (1999) Oxidation of the His-52 --> Leu mutant of cytochrome c peroxidase by p-nitroperoxybenzoic acid: role of the distal histidine in hydroperoxide activation. Biochemistry 38(47):15653-8
Moore GR, et al.  (1998) N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formation. Biochem J 332 ( Pt 2)():439-49
Matthis AL and Erman JE  (1995) Cytochrome c peroxidase-catalyzed oxidation of yeast iso-1 ferrocytochrome c by hydrogen peroxide. Ionic strength dependence of the steady-state parameters. Biochemistry 34(31):9985-90
Matthis AL, et al.  (1995) Oxidation of yeast iso-1 ferrocytochrome c by yeast cytochrome c peroxidase compounds I and II. Dependence upon ionic strength. Biochemistry 34(31):9991-9
Miller MA, et al.  (1995) Regulation of interprotein electron transfer by Trp 191 of cytochrome c peroxidase. Biochemistry 34(37):12048-58
Kuo MH and Grayhack E  (1994) A library of yeast genomic MCM1 binding sites contains genes involved in cell cycle control, cell wall and membrane structure, and metabolism. Mol Cell Biol 14(1):348-59
Corin AF, et al.  (1993) Effects of surface amino acid replacements in cytochrome c peroxidase on intracomplex electron transfer from cytochrome c. Biochemistry 32(11):2756-62
Stemp ED and Hoffman BM  (1993) Cytochrome c peroxidase binds two molecules of cytochrome c: evidence for a low-affinity, electron-transfer-active site on cytochrome c peroxidase. Biochemistry 32(40):10848-65
Pelletier H and Kraut J  (1992) Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c. Science 258(5089):1748-55
Cooper JM, et al.  (1991) Preparation and kinetic studies of immobilised yeast cytochrome c peroxidase. Biotechnol Appl Biochem 14(1):93-103
Hazzard JT, et al.  (1988) Effects of amino acid replacements in yeast iso-1 cytochrome c on heme accessibility and intracomplex electron transfer in complexes with cytochrome c peroxidase. Biochemistry 27(12):4445-51
Liang N, et al.  (1988) Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c. Science 240(4850):311-3
Erman JE, et al.  (1987) A covalent complex between horse heart cytochrome c and yeast cytochrome c peroxidase: kinetic properties. Biochim Biophys Acta 911(1):1-10