Protein Information

Name cytochrome c
Synonyms CYC; CYCS; Cytochrome C; HCS; Cytochrome Cs

Compound Information

Name cresol
CAS methylphenol

Reference List

PubMed Abstract RScore(About this table)
17223224 Aranha MM, Matos AR, Teresa Mendes A, Vaz Pinto V, Rodrigues CM, Arrabaca JD: Dinitro-o-cresol 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.


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.
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 oxygen species, and oxidizing ability. Inorg Chem. 2004 Nov 1;43(22):7127-40.


The formation of superoxide anion was spectrophotometrically confirmed using two independent methods, including the reduction of cytochrome c and the reduction of sodium 4-[3-(iodophenyl)-2-(4-nitrophenyl)-2H-5-tetrazolio]-1,3-benzene 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) ethanol 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 p-cresol methylhydroxylase. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9463-7.


The enzyme p-cresol methylhydroxylase [4-cresol: (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 NADH 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: p-Cresol methylhydroxylase. Biochem J. 1985 Jun 1;228(2):325-35.


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.
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 p-cresol 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-o-cresol: an ultrastructural and biochemical study. Ecotoxicol Environ Saf. 1991 Apr;21(2):109-27.


An increase in NADPH-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 p-cresol.
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 p-cresol 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-ubiquinone interaction in bovine heart mitochondrial succinate-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 p-cresol methylhydroxylase. Biochemistry. 1986 Oct 7;25(20):5975-81.


The flavocytochrome p-cresol 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.
2(0,0,0,2) Details
2990445 Bhattacharyya A, Tollin G, McIntire W, Singer TP: Laser-flash-photolysis studies of p-cresol methylhydroxylase. Biochem J. 1985 Jun 1;228(2):337-45.


p-Cresol 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 p-cresol oxidation) or to menaquinone (in the case of p-hydroxybenzyl alcohol 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 p-cresol methylhydroxylase from two strains of Pseudomonas putida. J Bacteriol. 1994 Oct;176(20):6349-61.


The structural genes for the flavoprotein subunit and cytochrome c subunit of p-cresol (4-methylphenol) 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.
1(0,0,0,1) Details