Other names published for CCP1: YKR066C
CCP1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
CCP1 - Protein Sequence Features (24)
| Reference | Other 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 | |
| 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 | |
| Konopka CA, et al. (2011) A yeast model for polyalanine-expansion aggregation and toxicity. Mol Biol Cell 22(12):1971-84 | |
| 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 | |
| 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 | |
| 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 | |
| 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 | |
| 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 | |
| Iffland A, et al. (2001) Changing the substrate specificity of cytochrome c peroxidase using directed evolution. Biochem Biophys Res Commun 286(1):126-32 | |
| Savenkova MI, et al. (2001) Expression, purification, characterization, and NMR studies of highly deuterated recombinant cytochrome c peroxidase. Biochemistry 40(40):12123-31 | |
| Zamocky M, et al. (2000) Common phylogeny of catalase-peroxidases and ascorbate peroxidases. Gene 256(1-2):169-82 | |
| 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 | |
| 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 | |
| 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 | |
| Satterlee JD, et al. (1990) Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235----Asn-235 mutant. Biochemistry 29(37):8797-804 | |
| Satterlee JD, et al. (1987) Proton hyperfine resonance assignments in cyanide-ligated cytochrome c peroxidase using the nuclear Overhauser effect. J Biol Chem 262(24):11578-83 | |
| Ho PS, et al. (1984) Kinetics and energetics of intramolecular electron transfer in yeast cytochrome c peroxidase. Biochemistry 23(18):4122-8 | |



