CCP1/YKR066C Literature Guide Help

Other names published for CCP1: YKR066C

CCP1 - Primary Literature (59)

Results: 1 - 30 of 59 records
   1  2 
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
Stevenson GP, et al.  (2012) Theoretical analysis of the two-electron transfer reaction and experimental studies with surface-confined cytochrome c peroxidase using large-amplitude Fourier transformed AC voltammetry. Langmuir 28(25):9864-77
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
Jensen GM and Goodin DB  (2011) Impact of Proximal and Distal Pocket Site-Directed Mutations on the Ferric/Ferrous Heme Redox Potential of Yeast Cytochrome--Peroxidase. Theor Chem Acc 130(4-6):1185-1196
Demir AB and Koc A  (2010) Assessment of chronological lifespan dependent molecular damages in yeast lacking mitochondrial antioxidant genes. Biochem Biophys Res Commun 400(1):106-10
Otero JM, et al.  (2010) Whole genome sequencing of Saccharomyces cerevisiae: from genotype to phenotype for improved metabolic engineering applications. BMC Genomics 11():723
Suppanz IE, et al.  (2009) The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria. Mol Biol Cell 20(2):572-80
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
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
Dabir DV, et al.  (2007) A role for cytochrome c and cytochrome c peroxidase in electron shuttling from Erv1. EMBO J 26(23):4801-11
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
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
Jiang H and English AM  (2006) Phenotypic analysis of the ccp1Delta and ccp1Delta-ccp1(W191F) mutant strains of Saccharomyces cerevisiae indicates that cytochrome c peroxidase functions in oxidative-stress signaling. J Inorg Biochem 100(12):1996-2008
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
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
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
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
Kwon M, et al.  (2003) Oxidative stresses elevate the expression of cytochrome c peroxidase in Saccharomyces cerevisiae. Biochim Biophys Acta 1623(1):1-5
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
Esser K, et al.  (2002) A novel two-step mechanism for removal of a mitochondrial signal sequence involves the mAAA complex and the putative rhomboid protease Pcp1. J Mol Biol 323(5):835-43
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
Iffland A, et al.  (2001) Changing the substrate specificity of cytochrome c peroxidase using directed evolution. Biochem Biophys Res Commun 286(1):126-32
Results: 1 - 30 of 59 records
   1  2