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1-methoxynaphthalene + H2O2
Russig's blue + 2 H2O
-
Substrates: -
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
?
Substrates: -
Products: -
?
2,2'-azino-bis(3-ethylenbenzthiazoline-6-sulfonic acid) + H2O2
?
2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) + H2O2
?
-
Substrates: -
Products: -
?
2-aminothiazole + H2O2
?
Substrates: modified enzyme
Products: -
?
acrylonitrile + H2O2
? + H2O
-
Substrates: -
Products: -
?
ascorbate + H2O2
dehydroascorbate + H2O
azo violet + H2O2
? + H2O
-
Substrates: -
Products: -
?
azurin + H2O2
oxidized azurin + ?
brillant blue + H2O2
? + H2O
-
Substrates: -
Products: -
?
ferrocyanide + H2O2
ferricyanide + OH-
ferrocytochrome c + CN-
?
-
Substrates: dominant binding pathway for H52L mutant, biphasic reaction
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + 2 H2O
-
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
ferrocytochrome c + HCN
?
-
Substrates: dominant binding pathway for wild-type enzyme
Products: -
?
ferrocytochrome c + menadione
ferricytochrome + oxidized menadione
-
Substrates: menadione can be substituted by 1,4-naphthoquinone
Products: -
?
ferrocytochrome c2 + H2O2
ferricytochrome c2 + OH-
-
Substrates: -
Products: -
?
ferrocytochrome c4 + H2O2
ferricytochrome c4 + OH-
-
Substrates: -
Products: -
?
ferrocytochrome c550 + H2O2
ferricytochrome c550 + H2O
-
Substrates: -
Products: -
r
ferrocytochrome c551 + H2O2
ferricytochrome c551 + OH-
ferrocytochrome c552 + H2O2
ferricytochrome c552 + OH-
ferrocytochrome c553 + H2O2
ferriytochrome c553 + OH-
-
Substrates: -
Products: -
?
ferrocytochrome c555 + H2O2
ferricytochrome c555 + OH-
-
Substrates: -
Products: -
?
ferrocytochrome c555 + H2O2
ferriytochrome c555 + OH-
-
Substrates: -
Products: -
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
horse ferrocytochrome c + H2O2
horse ferricytochrome c + H2O
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
hydroquinone + H2O2
benzoquinone + H2O
iso-1 ferrocytochrome c + H2O2
?
iso-1 ferrocytochrome c mutant C102T + H2O2
iso-1 ferricytochrome c mutant C102T + 2 H2O
-
Substrates: -
Products: -
?
iso-1-cytochrome c + ?
?
Substrates: -
Products: -
?
isoniazid + H2O2
?
Substrates: -
Products: -
?
NADH + H2O2
NAD+ + H2O
-
Substrates: -
Products: -
?
NADPH + H2O2
NADP+ + H2O
-
Substrates: -
Products: -
?
Reactive Black 5 + H2O2
? + H2O
-
Substrates: -
Products: -
?
reduced cytochrome c2 + H2O2
oxidized cytochrome c2 + H2O
reduced cytochrome c551 + H2O2
oxidized cytochrome c551 + H2O
-
Substrates: -
Products: -
?
reduced horse cytochrome c + H2O2
oxidized horse cytochrome c + H2O
reduced pseudoazurin + H2O2
oxidized pseudoazurin + H2O
-
Substrates: -
Products: -
?
Rhodobacter capsulatus ferrocytochrome c + H2O2
Rhodobacter capsulatus ferricytochrome c + H2O
Rhodobacter capsulatus ferrocytochrome c2 + H2O2
Rhodobacter capsulatus ferricytochrome c2 + H2O
veratryl alcohol + H2O2
veratraldehyde + H2O
-
Substrates: -
Products: -
?
yeast ferrocytochrome c + H2O2
yeast ferricytochrome c + H2O
-
Substrates: -
Products: -
r
additional information
?
-
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
Substrates: -
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
Substrates: 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
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
Substrates: -
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
Substrates: -
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
Substrates: -
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
Substrates: 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
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
Substrates: -
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
Substrates: -
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
Substrates: -
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
Substrates: -
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
Substrates: -
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
Substrates: -
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
Marinobacter nauticus
-
Substrates: -
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
Marinobacter nauticus 617
-
Substrates: -
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
-
Substrates: -
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
-
Substrates: -
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
-
Substrates: horse cytochrome c
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
-
Substrates: Pseudomonas aeruginosa cytochrome c-551
Products: -
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
-
Substrates: Pseudomonas aeruginosa cytochrome c-551
Products: -
?
2,2'-azino-bis(3-ethylenbenzthiazoline-6-sulfonic acid) + H2O2
?
Substrates: -
Products: -
?
2,2'-azino-bis(3-ethylenbenzthiazoline-6-sulfonic acid) + H2O2
?
Substrates: -
Products: -
?
ascorbate + H2O2
dehydroascorbate + H2O
-
Substrates: -
Products: -
?
ascorbate + H2O2
dehydroascorbate + H2O
Substrates: -
Products: -
?
ascorbate + H2O2
dehydroascorbate + H2O
-
Substrates: -
Products: -
?
azurin + H2O2
oxidized azurin + ?
-
Substrates: blue copper protein
Products: -
?
azurin + H2O2
oxidized azurin + ?
-
Substrates: blue copper protein
Products: -
?
cytochrome c + H2O2
?
-
Substrates: -
Products: -
?
cytochrome c + H2O2
?
Substrates: -
Products: -
?
cytochrome c + H2O2
?
-
Substrates: the reaction with hydrogen peroxide of the W51H/H52L mutant is much slower compared to those of the mutant W51H and W51H/H52W
Products: -
?
ferrocyanide + H2O2
ferricyanide + OH-
-
Substrates: -
Products: -
?
ferrocyanide + H2O2
ferricyanide + OH-
-
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: horse heart
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
Substrates: antioxidant defense
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
Substrates: antioxidant defense
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: horse heart
Products: -
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: horse heart
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
Substrates: investigation of the catalytic mechanism
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: horse heart
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: -
Products: -
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: -
Products: -
r
ferrocytochrome c + H2O2
ferricytochrome c + H2O
Substrates: -
Products: -
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
Substrates: -
Products: -
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: H2O2 can be substituted by ethyl peroxide
Products: -
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: yeast
Products: -
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: horse heart
Products: -
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: H2O2 can be substituted by ethyl peroxide
Products: -
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: yeast
Products: -
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
Substrates: horse heart
Products: -
ir
ferrocytochrome c551 + H2O2
ferricytochrome c551 + OH-
-
Substrates: -
Products: -
?
ferrocytochrome c551 + H2O2
ferricytochrome c551 + OH-
-
Substrates: -
Products: -
?
ferrocytochrome c552 + H2O2
ferricytochrome c552 + OH-
Marinobacter nauticus
-
Substrates: -
Products: -
?
ferrocytochrome c552 + H2O2
ferricytochrome c552 + OH-
Marinobacter nauticus 617
-
Substrates: -
Products: -
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
-
Substrates: -
Products: -
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
Substrates: -
Products: -
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
-
Substrates: -
Products: -
?
horse ferrocytochrome c + H2O2
horse ferricytochrome c + H2O
-
Substrates: -
Products: -
r
horse ferrocytochrome c + H2O2
horse ferricytochrome c + H2O
-
Substrates: -
Products: -
r
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
-
Substrates: -
Products: -
?
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
-
Substrates: -
Products: -
?
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
-
Substrates: -
Products: -
?
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
-
Substrates: -
Products: -
r
hydroquinone + H2O2
benzoquinone + H2O
-
Substrates: -
Products: -
?
hydroquinone + H2O2
benzoquinone + H2O
-
Substrates: -
Products: -
?
iso-1 ferrocytochrome c + H2O2
?
-
Substrates: -
Products: -
?
iso-1 ferrocytochrome c + H2O2
?
-
Substrates: C102T
Products: -
?
pyrogallol + H2O2
?
-
Substrates: -
Products: -
?
pyrogallol + H2O2
?
-
Substrates: -
Products: -
?
reduced cytochrome c2 + H2O2
oxidized cytochrome c2 + H2O
-
Substrates: -
Products: -
?
reduced cytochrome c2 + H2O2
oxidized cytochrome c2 + H2O
-
Substrates: -
Products: -
?
reduced horse cytochrome c + H2O2
oxidized horse cytochrome c + H2O
-
Substrates: -
Products: -
?
reduced horse cytochrome c + H2O2
oxidized horse cytochrome c + H2O
-
Substrates: -
Products: -
?
Rhodobacter capsulatus ferrocytochrome c + H2O2
Rhodobacter capsulatus ferricytochrome c + H2O
-
Substrates: -
Products: -
r
Rhodobacter capsulatus ferrocytochrome c + H2O2
Rhodobacter capsulatus ferricytochrome c + H2O
-
Substrates: -
Products: -
r
Rhodobacter capsulatus ferrocytochrome c2 + H2O2
Rhodobacter capsulatus ferricytochrome c2 + H2O
-
Substrates: -
Products: -
r
Rhodobacter capsulatus ferrocytochrome c2 + H2O2
Rhodobacter capsulatus ferricytochrome c2 + H2O
-
Substrates: -
Products: -
r
additional information
?
-
-
Substrates: Leishmania major peroxidase (LmP) exhibits both ascorbate and cytochrome c peroxidase activities, but cytochrome c is the natural substrate
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: no oxidation of ferrocytochrome c of bacteria, no mammalian ferrocytochrome b, b5, c1
Products: -
?
additional information
?
-
-
Substrates: Ccp1 functions as a terminal electron acceptor for sulfhydryl oxidase Erv1
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: formation of a covalent link from Trp51 to the heme on reaction with H2O2
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: no oxidation of ferrocytochrome c of bacteria, no mammalian ferrocytochrome b, b5, c1
Products: -
?
additional information
?
-
-
Substrates: menaquinol pool-based origin of electrons that are transferred to CcpA
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
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