CCP1/YKR066C Literature Guide Help

Other names published for CCP1: YKR066C

CCP1 - Substrates/Ligands/Cofactors (29)

ReferenceOther Genes Addressed
Bidwai AK, et al.  (2013) Apolar distal pocket mutants of yeast cytochrome c peroxidase: Hydrogen peroxide reactivity and cyanide binding of the TriAla, TriVal, and TriLeu variants. Biochim Biophys Acta 1834(1):137-48
De Wael K, et al.  (2012) Electrochemical determination of hydrogen peroxide with cytochrome c peroxidase and horse heart cytochrome c entrapped in a gelatin hydrogel. Bioelectrochemistry 83():15-8
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
Kang SA, et al.  (2006) Solvent isotope effects on interfacial protein electron transfer in crystals and electrode films. J Am Chem Soc 128(7):2346-55
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
Bhaskar B, et al.  (2003) A novel heme and peroxide-dependent tryptophan-tyrosine cross-link in a mutant of cytochrome c peroxidase. J Mol Biol 328(1):157-66
Bidwai A, et al.  (2003) Cyanide binding to cytochrome c peroxidase (H52L). Biochemistry 42(36):10764-71
Bonagura CA, et al.  (2003) High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase. Biochemistry 42(19):5600-8
Feng M, et al.  (2003) Resonance Raman spectroscopy of cytochrome c peroxidase variants that mimic manganese peroxidase. J Biol Inorg Chem 8(7):699-706
Zhang H, et al.  (2002) Radical formation at Tyr39 and Tyr153 following reaction of yeast cytochrome c peroxidase with hydrogen peroxide. Biochemistry 41(46):13507-13
Iffland A, et al.  (2001) Changing the substrate specificity of cytochrome c peroxidase using directed evolution. Biochem Biophys Res Commun 286(1):126-32
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
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
Pond AE, et al.  (1999) Influence of protein environment on magnetic circular dichroism spectral properties of ferric and ferrous ligand complexes of yeast cytochrome c peroxidase. Biospectroscopy 5(5 Suppl):S42-52
Pond AE, et al.  (1999) Magnetic circular dichroism studies of the active site heme coordination sphere of exogenous ligand-free ferric cytochrome c peroxidase from yeast: effects of sample history and pH. J Inorg Biochem 76(3-4):165-74
Miller MA, et al.  (1995) Regulation of interprotein electron transfer by Trp 191 of cytochrome c peroxidase. Biochemistry 34(37):12048-58
Fox T, et al.  (1994) Fluorescence investigation of yeast cytochrome c peroxidase oxidation by H2O2 and enzyme activities of the oxidized enzyme. Biochemistry 33(1):186-91
Fulop V, et al.  (1994) Laue diffraction study on the structure of cytochrome c peroxidase compound I. Structure 2(3):201-8
Cooper JM, et al.  (1991) Preparation and kinetic studies of immobilised yeast cytochrome c peroxidase. Biotechnol Appl Biochem 14(1):93-103
Edwards SL and Poulos TL  (1990) Ligand binding and structural perturbations in cytochrome c peroxidase. A crystallographic study. J Biol Chem 265(5):2588-95
Goodin DB, et al.  (1987) The peroxide complex of yeast cytochrome c peroxidase contains two distinct radical species, neither of which resides at methionine 172 or tryptophan 51. J Biol Chem 262(16):7719-24
Ho PS, et al.  (1984) Kinetics and energetics of intramolecular electron transfer in yeast cytochrome c peroxidase. Biochemistry 23(18):4122-8
Ho PS, et al.  (1983) Control of the transfer of oxidizing equivalents between heme iron and free radical site in yeast cytochrome c peroxidase. J Biol Chem 258(7):4356-63
Poulos TL, et al.  (1978) Crystallographic determination of the heme orientation and location of the cyanide binding site in yeast cytochrome c peroxidase. J Biol Chem 253(10):3730-5
Kang CH, et al.  (1977) Steady state kinetics and binding of eukaryotic cytochromes c with yeast cytochrome c peroxidase. J Biol Chem 252(3):919-26
Yonetani T and Ray GS  (1966) Studies on cytochrome c peroxidase. 3. Kinetics of the peroxidatic oxidation of ferrocytochrome c catalyzed by cytochrome c peroxidase. J Biol Chem 241(3):700-6