Name | cytochrome c |
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Synonyms | CYC; CYCS; Cytochrome C; HCS; Cytochrome Cs |
Name | cresol |
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CAS | methylphenol |
PubMed | Abstract | RScore(About this table) | |
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17223224 | Aranha MM, Matos AR, Teresa Mendes A, Vaz Pinto V, Rodrigues CM, Arrabaca JD: Dinitro- In addition, specific colorimetric assays and immunoblot analysis revealed activation of caspase-3-like proteins and release of cytochrome c from mitochondria, respectively, confirming the apoptotic-like phenotype. |
induces apoptosis-like cell death but not alternative oxidase expression in soybean cells. J Plant Physiol. 2007 Jun;164(6):675-84. Epub 2007 Jan 16.1(0,0,0,1) | Details |
15500351 | Kanamori K, Nishida K, Miyata N, Shimoyama T, Hata K, Mihara C, Okamoto K, Abe Y, Hayakawa S, Matsugo S: Mononuclear and dinuclear monoperoxovanadium (v) complexes with a hetero ligand. 1.(1) Self-decomposition reaction, detection of reactive species, and oxidizing ability. Inorg Chem. 2004 Nov 1;43(22):7127-40. The formation of was spectrophotometrically confirmed using two independent methods, including the reduction of cytochrome c and the reduction of 4-[3-(iodophenyl)-2- -2H-5-tetrazolio]-1,3- disulfonate (WST-1). |
1(0,0,0,1) | Details |
2556994 | Reeve CD, Carver MA, Hopper DJ: The purification and characterization of 4-ethylphenol methylenehydroxylase, a flavocytochrome from Pseudomonas putida JD1. Biochem J. 1989 Oct 15;263(2):431-7. The enzyme consists of two flavoprotein subunits each of Mr 50,000 and two cytochrome c subunits each of Mr 10,000. |
1(0,0,0,1) | Details |
1697166 | Reeve CD, Carver MA, Hopper DJ: Stereochemical aspects of the oxidation of 4-ethylphenol by the bacterial enzyme 4-ethylphenol methylenehydroxylase. Biochem J. 1990 Aug 1;269(3):815-9. The enantiomer of 1-(4-hydroxyphenyl) produced by 4EPMH was R (+) when horse heart cytochrome c or azurin was used as electron acceptor for the enzyme. |
1(0,0,0,1) | Details |
1946360 | McLendon GL, Bagby S, Charman JA, Driscoll PC, McIntire WS, Mathews FS, Hill HA: Subunit interactions change the heme active-site geometry in methylhydroxylase. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9463-7. The enzyme methylhydroxylase (acceptor) oxidoreductase (methyl-hydroxylating), EC 1.17.99.1] contains two subunits: a cytochrome c (electron transfer) subunit (cytochrome cpc) and a flavin (catalytic) subunit. |
1(0,0,0,1) | Details |
7578004 | Newman LM, Wackett LP: Purification and characterization of toluene 2-monooxygenase from Burkholderia cepacia G4. Biochemistry. 1995 Oct 31;34(43):14066-76. The 40 kDa flavo-iron-sulfur protein oxidized and transferred electrons to cytochrome c, dyes, and the alpha 2 beta 2 gamma 2 component. |
1(0,0,0,1) | Details |
2990444 | McIntire W, Hopper DJ, Singer TP: One of these is the fact that its flavoprotein and cytochrome c subunits may be reversibly dissociated with ease, with full regeneration of the activity and its native properties on recombining the components. |
methylhydroxylase. Biochem J. 1985 Jun 1;228(2):325-35.1(0,0,0,1) | Details |
8537385 | Kim J, Fuller JH, Kuusk V, Cunane L, Chen ZW, Mathews FS, McIntire WS: The cytochrome subunit is necessary for covalent FAD attachment to the flavoprotein subunit of methylhydroxylase. J Biol Chem. 1995 Dec 29;270(52):31202-9. The apoflavoprotein has been expressed in E. coli in the absence of the beta cytochrome c subunit and purified. |
1(0,0,0,1) | Details |
2065626 | Braunbeck T, Volkl A: Induction of biotransformation in the liver of Eel (Anguilla anguilla L.) by sublethal exposure to dinitro- an ultrastructural and biochemical study. Ecotoxicol Environ Saf. 1991 Apr;21(2):109-27. An increase in -cytochrome c reductase and cytochrome P450 as well as UDP-glucuronyltransferase and arylsulfotransferase activities in the microsomal fraction document an induction of hepatic biotransformation as a functional correlate to SER proliferation. |
1(0,0,0,1) | Details |
7918458 | Banci L, Carloni P, Savellini GG: Molecular dynamics studies on peroxidases: a structural model for horseradish peroxidase and a substrate adduct. Biochemistry. 1994 Oct 18;33(41):12356-66. Molecular dynamics (MD) calculations are performed on cytochrome c peroxidase (CcP) and on horseradish peroxidase, isoenzyme C (HRP), and its substrate adduct with |
1(0,0,0,1) | Details |
1649169 | Van Beeumen JJ, Demol H, Samyn B, Bartsch RG, Meyer TE, Dolata MM, Cusanovich MA: Covalent structure of the diheme cytochrome subunit and amino-terminal sequence of the flavoprotein subunit of flavocytochrome c from Chromatium vinosum. J Biol Chem. 1991 Jul 15;266(20):12921-31. Although the locations of the heme binding sites and the heme ligands suggest that the cytochrome subunit is the result of gene doubling of a type I cytochrome c, as found with Azotobacter cytochrome c4, the extremely low similarity of only 7% between the two halves of the Chromatium FC heme subunit rather suggests that gene fusion is at the evolutionary origin of this cytochrome. |
1(0,0,0,1) | Details |
6309572 | Hopper DJ: Redox potential of the cytochrome c in the flavocytochrome methylhydroxylase. FEBS Lett. 1983 Sep 5;161(1):100-2. |
3(0,0,0,3) | Details |
1657937 | Yang F, Yu L, He DY, Yu CA: Protein-interaction in bovine heart mitochondrial -cytochrome c reductase. J Biol Chem. 1991 Nov 5;266(31):20863-9. |
3(0,0,0,3) | Details |
3790500 | McIntire W, Singer TP, Smith AJ, Mathews FS: Amino acid and sequence analysis of the cytochrome and flavoprotein subunits of The flavocytochrome methylhydroxylase from Pseudomonas putida has been reported to have a Mr of 114,000 and to consist of two subunits, a flavoprotein and a cytochrome c, each with a Mr of 58,000. |
methylhydroxylase. Biochemistry. 1986 Oct 7;25(20):5975-81.2(0,0,0,2) | Details |
2990445 | Bhattacharyya A, Tollin G, McIntire W, Singer TP: Laser-flash-photolysis studies of methylhydroxylase. Biochem J. 1985 Jun 1;228(2):337-45. methylhydroxylase, a heterodimer consisting of one flavoprotein subunit and one cytochrome c subunit, may be resolved into its subunits, and the holoenzyme may then be fully reconstituted from the pure subunits. |
2(0,0,0,2) | Details |
17449613 | Peters F, Heintz D, Johannes J, van Dorsselaer A, Boll M: Genes, enzymes, and regulation of para-cresol metabolism in Geobacter metallireducens. J Bacteriol. 2007 Jul;189(13):4729-38. Epub 2007 Apr 20. We propose that the unusual asymmetric architecture and the membrane association of PCMH might be important for alternative electron transfer routes to either cytochrome c (in the case of oxidation) or to (in the case of p-hydroxybenzyl oxidation). |
1(0,0,0,1) | Details |
7929007 | Kim J, Fuller JH, Cecchini G, McIntire WS: Cloning, sequencing, and expression of the structural genes for the cytochrome and flavoprotein subunits of Pseudomonas putida. J Bacteriol. 1994 Oct;176(20):6349-61. The structural genes for the flavoprotein subunit and cytochrome c subunit of methylhydroxylase (PCMH) from Pseudomonas putida NCIMB 9869 (National Collection of Industrial and Marine Bacteria, Aberdeen, Scotland) and P. putida NCIMB 9866 were cloned and sequenced. |
methylhydroxylase from two strains of 1(0,0,0,1) | Details |