CCP1/YKR066C Literature Guide Help

Other names published for CCP1: YKR066C

CCP1 - Protein Physical Properties (57)

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
Cheng JS, et al.  (2009) Proteomic insights into adaptive responses of Saccharomyces cerevisiae to the repeated vacuum fermentation. Appl Microbiol Biotechnol 83(5):909-23
Volkov AN, et al.  (2009) Binding hot spot in the weak protein complex of physiological redox partners yeast cytochrome C and cytochrome C peroxidase. J Mol Biol 385(3):1003-13
Heimdal J, et al.  (2008) Protonation of the proximal histidine ligand in heme peroxidases. J Phys Chem B 112(8):2501-10
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
DiCarlo CM, et al.  (2007) Effect of active site and surface mutations on the reduction potential of yeast cytochrome c peroxidase and spectroscopic properties of the oxidized and reduced enzyme. J Inorg Biochem 101(4):603-13
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
Nakani S, et al.  (2006) Characterization of four covalently-linked yeast cytochrome c/cytochrome c peroxidase complexes: Evidence for electrostatic interaction between bound cytochrome c molecules. Biochemistry 45(48):14371-8
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
Guo M, et al.  (2004) Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link. Proc Natl Acad Sci U S A 101(16):5940-5
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
Bidwai A, et al.  (2003) Cyanide binding to cytochrome c peroxidase (H52L). Biochemistry 42(36):10764-71
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
Satterlee JD, et al.  (2003) Temperature, pH, and solvent isotope dependent properties of the active sites of resting-state and cyanide-ligated recombinant cytochrome c peroxidase (H52L) revealed by proton hyperfine resonance spectra. Biochemistry 42(36):10772-82
Mei H, et al.  (2002) Role of the low-affinity binding site in electron transfer from cytochrome C to cytochrome C peroxidase. Biochemistry 41(12):3968-76
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
Hirst J, et al.  (2001) Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 2. Effects on heme coordination and function. Biochemistry 40(5):1274-83
Iffland A, et al.  (2001) Changing the substrate specificity of cytochrome c peroxidase using directed evolution. Biochem Biophys Res Commun 286(1):126-32
Morar AS, et al.  (2001) Effects of crowding by mono-, di-, and tetrasaccharides on cytochrome c-cytochrome c peroxidase binding: comparing experiment to theory. Biochemistry 40(1):281-5
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
Savenkova MI, et al.  (2001) Expression, purification, characterization, and NMR studies of highly deuterated recombinant cytochrome c peroxidase. Biochemistry 40(40):12123-31
Worrall JA, et al.  (2001) Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by [15N, 1H] heteronuclear NMR spectroscopy. Biochemistry 40(24):7069-76
Hirota S, et al.  (2000) Interactions of cytochrome c peroxidase with lysine peptides. Biochem Biophys Res Commun 268(2):395-7
Gengenbach A, et al.  (1999) Redesign of cytochrome c peroxidase into a manganese peroxidase: role of tryptophans in peroxidase activity. Biochemistry 38(35):11425-32
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