1.11.1.5 1-methoxynaphthalene + H2O2 - Saccharomyces cerevisiae Russig's blue + 2 H2O - ? 425272 1.11.1.5 2 ferrocytochrome c + H2O2 - Paracoccus denitrificans 2 ferricytochrome c + H2O - ? 380884 1.11.1.5 2 ferrocytochrome c + H2O2 - Nitrosomonas europaea 2 ferricytochrome c + H2O - ? 380884 1.11.1.5 2 ferrocytochrome c + H2O2 - Marinobacter nauticus 2 ferricytochrome c + H2O - ? 380884 1.11.1.5 2 ferrocytochrome c + H2O2 - Geobacter sulfurreducens 2 ferricytochrome c + H2O - ? 380884 1.11.1.5 2 ferrocytochrome c + H2O2 horse cytochrome c Paracoccus denitrificans 2 ferricytochrome c + H2O - ? 380884 1.11.1.5 2 ferrocytochrome c + H2O2 Pseudomonas aeruginosa cytochrome c-551 Pseudomonas stutzeri 2 ferricytochrome c + H2O - ? 380884 1.11.1.5 2 ferrocytochrome c + H2O2 - Marinobacter nauticus 617 2 ferricytochrome c + H2O - ? 380884 1.11.1.5 2 ferrocytochrome c + H2O2 Pseudomonas aeruginosa cytochrome c-551 Pseudomonas stutzeri 9721 2 ferricytochrome c + H2O - ? 380884 1.11.1.5 2 ferrocytochrome c + H2O2 - Saccharomyces cerevisiae 2 ferricytochrome c + 2 H2O - ? 424460 1.11.1.5 2 ferrocytochrome c + H2O2 - Nitrosomonas europaea 2 ferricytochrome c + 2 H2O - ? 424460 1.11.1.5 2 ferrocytochrome c + H2O2 - Leishmania major 2 ferricytochrome c + 2 H2O - ? 424460 1.11.1.5 2 ferrocytochrome c + H2O2 - Shewanella oneidensis 2 ferricytochrome c + 2 H2O - ? 424460 1.11.1.5 2 ferrocytochrome c + H2O2 - Zymomonas mobilis 2 ferricytochrome c + 2 H2O - ? 424460 1.11.1.5 2 ferrocytochrome c + H2O2 activity with wild-type cytochrome c from Leishmania major and reduced activity with mutant cytochrome c R24A and K98A, no activity with cyt c mutant R24A/K98A Leishmania major 2 ferricytochrome c + 2 H2O - ? 424460 1.11.1.5 2 ferrocytochrome c + H2O2 via intermediate compound I formation. The rate-limiting step in CcP compound I formation is the binding of hydrogen peroxide to the heme iron rather than the redox chemistry involved in compound I formation Saccharomyces cerevisiae 2 ferricytochrome c + 2 H2O - ? 424460 1.11.1.5 2 ferrocytochrome c + H2O2 - Saccharomyces cerevisiae ATCC 204508 2 ferricytochrome c + 2 H2O - ? 424460 1.11.1.5 2 ferrocytochrome c + H2O2 - Saccharomyces cerevisiae Red Star 2 ferricytochrome c + 2 H2O - ? 424460 1.11.1.5 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2 - Geobacter sulfurreducens ? - ? 407815 1.11.1.5 2,2'-azino-bis(3-ethylenbenzthiazoline-6-sulfonic acid) + H2O2 - Geobacter sulfurreducens ? - ? 425355 1.11.1.5 2,2'-azino-bis(3-ethylenbenzthiazoline-6-sulfonic acid) + H2O2 - Geobacter sulfurreducens DSM 12127 ? - ? 425355 1.11.1.5 2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) + H2O2 - Shewanella oneidensis ? - ? 425361 1.11.1.5 2-aminothiazole + H2O2 modified enzyme Saccharomyces cerevisiae ? - ? 260343 1.11.1.5 acrylonitrile + H2O2 - Saccharomyces cerevisiae ? + H2O - ? 441022 1.11.1.5 ascorbate + H2O2 - Saccharomyces pastorianus dehydroascorbate + H2O - ? 260337 1.11.1.5 ascorbate + H2O2 - Saccharomyces cerevisiae dehydroascorbate + H2O - ? 260337 1.11.1.5 azo violet + H2O2 - Saccharomyces cerevisiae ? + H2O - ? 441085 1.11.1.5 azurin + H2O2 blue copper protein Pseudomonas aeruginosa oxidized azurin + ? - ? 260334 1.11.1.5 azurin + H2O2 blue copper protein Pseudomonas denitrificans (nom. rej.) oxidized azurin + ? - ? 260334 1.11.1.5 brillant blue + H2O2 - Saccharomyces cerevisiae ? + H2O - ? 441147 1.11.1.5 cytochrome c + H2O2 - Saccharomyces cerevisiae ? - ? 404752 1.11.1.5 cytochrome c + H2O2 the reaction with hydrogen peroxide of the W51H/H52L mutant is much slower compared to those of the mutant W51H and W51H/H52W Saccharomyces cerevisiae ? - ? 404752 1.11.1.5 ferrocyanide + H2O2 - Saccharomyces pastorianus ferricyanide + OH- - ? 260341 1.11.1.5 ferrocyanide + H2O2 - Saccharomyces cerevisiae ferricyanide + OH- - ? 260341 1.11.1.5 ferrocytochrome c + CN- dominant binding pathway for H52L mutant, biphasic reaction Saccharomyces cerevisiae ? - ? 376799 1.11.1.5 ferrocytochrome c + H2O2 - Escherichia coli ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 - Saccharomyces cerevisiae ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 - Saccharomyces cerevisiae ferricytochrome c + H2O - ir 260331 1.11.1.5 ferrocytochrome c + H2O2 - Saccharomyces cerevisiae ferricytochrome c + H2O - r 260331 1.11.1.5 ferrocytochrome c + H2O2 - Pseudomonas aeruginosa ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 - Pseudomonas stutzeri ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 - Nitrosomonas europaea ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 - Neisseria gonorrhoeae ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 - Paracoccus pantotrophus ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 - Campylobacter jejuni ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 - Cryptococcus neoformans ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 H2O2 can be substituted by ethyl peroxide Saccharomyces pastorianus ferricytochrome c + H2O - ir 260331 1.11.1.5 ferrocytochrome c + H2O2 H2O2 can be substituted by ethyl peroxide Saccharomyces cerevisiae ferricytochrome c + H2O - ir 260331 1.11.1.5 ferrocytochrome c + H2O2 yeast Saccharomyces pastorianus ferricytochrome c + H2O - ir 260331 1.11.1.5 ferrocytochrome c + H2O2 yeast Saccharomyces cerevisiae ferricytochrome c + H2O - ir 260331 1.11.1.5 ferrocytochrome c + H2O2 horse heart Paracoccus denitrificans ferricytochrome c + H2O - ir 260331 1.11.1.5 ferrocytochrome c + H2O2 horse heart Saccharomyces pastorianus ferricytochrome c + H2O - ir 260331 1.11.1.5 ferrocytochrome c + H2O2 horse heart Saccharomyces cerevisiae ferricytochrome c + H2O - ir 260331 1.11.1.5 ferrocytochrome c + H2O2 horse heart Pseudomonas aeruginosa ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 horse heart Rhodobacter capsulatus ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 horse heart Acidithiobacillus thiooxidans ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 antioxidant defense Cryptococcus neoformans ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 investigation of the catalytic mechanism Pseudomonas aeruginosa ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 - Paracoccus pantotrophus LMD 52.44 ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 - Campylobacter jejuni 81-176 ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 - Cryptococcus neoformans H99 ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 antioxidant defense Cryptococcus neoformans H99 ferricytochrome c + H2O - ? 260331 1.11.1.5 ferrocytochrome c + H2O2 - Saccharomyces cerevisiae ferricytochrome c + 2 H2O - ? 388688 1.11.1.5 ferrocytochrome c + HCN dominant binding pathway for wild-type enzyme Saccharomyces cerevisiae ? - ? 376800 1.11.1.5 ferrocytochrome c + menadione menadione can be substituted by 1,4-naphthoquinone Acidithiobacillus thiooxidans ferricytochrome + oxidized menadione - ? 260336 1.11.1.5 ferrocytochrome c2 + H2O2 - Rhodobacter capsulatus ferricytochrome c2 + OH- - ? 260345 1.11.1.5 ferrocytochrome c4 + H2O2 - Pseudomonas denitrificans (nom. rej.) ferricytochrome c4 + OH- - ? 260332 1.11.1.5 ferrocytochrome c550 + H2O2 - Paracoccus denitrificans ferricytochrome c550 + H2O - r 451198 1.11.1.5 ferrocytochrome c551 + H2O2 - Pseudomonas aeruginosa ferricytochrome c551 + OH- - ? 260330 1.11.1.5 ferrocytochrome c551 + H2O2 - Pseudomonas denitrificans (nom. rej.) ferricytochrome c551 + OH- - ? 260330 1.11.1.5 ferrocytochrome c552 + H2O2 - Marinobacter nauticus ferricytochrome c552 + OH- - ? 260344 1.11.1.5 ferrocytochrome c552 + H2O2 - Marinobacter nauticus 617 ferricytochrome c552 + OH- - ? 260344 1.11.1.5 ferrocytochrome c553 + H2O2 - Nitrosomonas europaea ferriytochrome c553 + OH- - ? 260347 1.11.1.5 ferrocytochrome c555 + H2O2 - Methylococcus capsulatus ferriytochrome c555 + OH- - ? 260342 1.11.1.5 ferrocytochrome c555 + H2O2 - Paracoccus denitrificans ferricytochrome c555 + OH- - ? 260346 1.11.1.5 guaiacol + H2O2 - Saccharomyces pastorianus 2-methoxy-cyclohexa-2,5-dienone + H2O - ? 260339 1.11.1.5 guaiacol + H2O2 - Saccharomyces cerevisiae 2-methoxy-cyclohexa-2,5-dienone + H2O - ? 260339 1.11.1.5 horse ferrocytochrome c + H2O2 - Rhodobacter capsulatus horse ferricytochrome c + H2O - r 451199 1.11.1.5 horse ferrocytochrome c + H2O2 - Rhodobacter capsulatus B10 horse ferricytochrome c + H2O - r 451199 1.11.1.5 horse heart ferrocytochrome c + H2O2 - Saccharomyces cerevisiae horse heart ferricytochrome c + H2O - r 397440 1.11.1.5 horse heart ferrocytochrome c + H2O2 - Paracoccus pantotrophus horse heart ferricytochrome c + H2O - ? 397440 1.11.1.5 horse heart ferrocytochrome c + H2O2 - Paracoccidioides brasiliensis horse heart ferricytochrome c + H2O - ? 397440 1.11.1.5 horse heart ferrocytochrome c + H2O2 - Paracoccidioides brasiliensis Pb01 / ATCC MYA 826 horse heart ferricytochrome c + H2O - ? 397440 1.11.1.5 hydroquinone + H2O2 - Saccharomyces pastorianus benzoquinone + H2O - ? 260340 1.11.1.5 hydroquinone + H2O2 - Saccharomyces cerevisiae benzoquinone + H2O - ? 260340 1.11.1.5 iso-1 ferrocytochrome c + H2O2 - Saccharomyces cerevisiae ? - ? 397476 1.11.1.5 iso-1 ferrocytochrome c + H2O2 C102T Saccharomyces cerevisiae ? - ? 397476 1.11.1.5 iso-1 ferrocytochrome c mutant C102T + H2O2 - Saccharomyces cerevisiae iso-1 ferricytochrome c mutant C102T + 2 H2O - ? 426514 1.11.1.5 iso-1-cytochrome c + ? - Saccharomyces cerevisiae ? - ? 409604 1.11.1.5 isoniazid + H2O2 - Saccharomyces cerevisiae ? - ? 370999 1.11.1.5 additional information no oxidation of ferrocytochrome c of bacteria, no mammalian ferrocytochrome b, b5, c1 Saccharomyces pastorianus ? - ? 89 1.11.1.5 additional information no oxidation of ferrocytochrome c of bacteria, no mammalian ferrocytochrome b, b5, c1 Saccharomyces cerevisiae ? - ? 89 1.11.1.5 additional information Ccp1 functions as a terminal electron acceptor for sulfhydryl oxidase Erv1 Saccharomyces cerevisiae ? - ? 89 1.11.1.5 additional information investigation of the binding hot-spot residue Y39 in the weak protein complex of physiological redox partners yeast iso-1-cytochrome c and cytochrome c peroxidase, cytochrome c and cytochrome c peroxidase binding parameters Saccharomyces cerevisiae ? - ? 89 1.11.1.5 additional information formation of a covalent link from Trp51 to the heme on reaction with H2O2 Saccharomyces cerevisiae ? - ? 89 1.11.1.5 additional information investigation of an engineered channel mutant with the surrogate peptide (N-benzimidazole-propionic acid)-Gly-Ala-Ala (BzGAA), complete loss of functional activity in the BzGAA/ET channel mutant strongly supports proposals that the Trp-191 radical intermediate is required for efficient turnover of cyt c via the proposed ET pathway Saccharomyces cerevisiae ? - ? 89 1.11.1.5 additional information Leishmania major peroxidase (LmP) exhibits both ascorbate and cytochrome c peroxidase activities, but cytochrome c is the natural substrate Leishmania major ? - ? 89 1.11.1.5 additional information menaquinol pool-based origin of electrons that are transferred to CcpA Shewanella oneidensis ? - ? 89 1.11.1.5 additional information Leishmania major cytochrome c has an electropositive surface surrounding the exposed heme edge that serves as the docking site with redox partners. Kinetic assays performed with Leishmania major cytochrome c and the enzyme show that it is a much better substrate for LmP than horse heart cytochrome c Leishmania major ? - ? 89 1.11.1.5 additional information residues Tyr71 and Tyr236 contribute primarily to the EPR spectrum of the tyrosyl radical. The heme distal-side Trp51 is involved in the intramolecular electron transfer between Tyr71 and the heme and formation of Tyr71 and Tyr236 radicals is independent of the [Fe(IV)=O Trp191+] radical intermediate. Tyr71 radical is the reactive species with the guaiacol substrate. Surface-exposed residue Tyr236 is the other radical site Saccharomyces cerevisiae ? - ? 89 1.11.1.5 additional information the rate-limiting step involves a proton-coupled single electron reduction of a high valent iron species centered on the low-potential heme. Reduction shifts the pKa's of at least two amino acids. Loop 1 shifts during the rate-limiting step, changing the environment of residue His81 Shewanella oneidensis ? - ? 89 1.11.1.5 NADH + H2O2 - Acidithiobacillus thiooxidans NAD+ + H2O - ? 260333 1.11.1.5 NADPH + H2O2 - Acidithiobacillus thiooxidans NADP+ + H2O - ? 260335 1.11.1.5 pyrogallol + H2O2 - Saccharomyces pastorianus ? - ? 260338 1.11.1.5 pyrogallol + H2O2 - Saccharomyces cerevisiae ? - ? 260338 1.11.1.5 Reactive Black 5 + H2O2 - Saccharomyces cerevisiae ? + H2O - ? 398245 1.11.1.5 reduced cytochrome c2 + H2O2 - Rhodobacter capsulatus oxidized cytochrome c2 + H2O - ? 382720 1.11.1.5 reduced cytochrome c2 + H2O2 - Rhodobacter capsulatus B10 oxidized cytochrome c2 + H2O - ? 382720 1.11.1.5 reduced cytochrome c551 + H2O2 - Pseudomonas aeruginosa oxidized cytochrome c551 + H2O - ? 398249 1.11.1.5 reduced horse cytochrome c + H2O2 - Rhodobacter capsulatus oxidized horse cytochrome c + H2O - ? 382722 1.11.1.5 reduced horse cytochrome c + H2O2 - Rhodobacter capsulatus B10 oxidized horse cytochrome c + H2O - ? 382722 1.11.1.5 reduced pseudoazurin + H2O2 - Paracoccus pantotrophus oxidized pseudoazurin + H2O - ? 398251 1.11.1.5 Rhodobacter capsulatus ferrocytochrome c + H2O2 - Rhodobacter capsulatus Rhodobacter capsulatus ferricytochrome c + H2O - r 451200 1.11.1.5 Rhodobacter capsulatus ferrocytochrome c + H2O2 - Rhodobacter capsulatus B10 Rhodobacter capsulatus ferricytochrome c + H2O - r 451200 1.11.1.5 Rhodobacter capsulatus ferrocytochrome c2 + H2O2 - Rhodobacter capsulatus Rhodobacter capsulatus ferricytochrome c2 + H2O - r 453831 1.11.1.5 Rhodobacter capsulatus ferrocytochrome c2 + H2O2 - Rhodobacter capsulatus B10 Rhodobacter capsulatus ferricytochrome c2 + H2O - r 453831 1.11.1.5 veratryl alcohol + H2O2 - Saccharomyces cerevisiae veratraldehyde + H2O - ? 442069 1.11.1.5 yeast ferrocytochrome c + H2O2 - Saccharomyces cerevisiae yeast ferricytochrome c + H2O - r 453832