1.11.1.5: cytochrome-c peroxidase

This is an abbreviated version!
For detailed information about cytochrome-c peroxidase, go to the full flat file.

Word Map on EC 1.11.1.5

Reaction

2 ferrocytochrome c +

H2O2
=
2 ferricytochrome c
+ 2 H2O

Synonyms

apocytochrome c peroxidase, BCcP, CCP, CCP1, CcpA, Cjj0382, CytC, cytochrome c iso-1, cytochrome c peroxidase, cytochrome c-551 peroxidase, cytochrome c-H2O oxidoreductase, cytochrome peroxidase, di-heme cytochrome c peroxidase, diheme cytochrome c peroxidase, diheme cytochrome c5 peroxidase CcpA, DocA, LmP, MacA, mesocytochrome c peroxidase azide, mesocytochrome c peroxidase cyanate, mesocytochrome c peroxidase cyanide, peroxidase, cytochrome c, Psa CcP

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.5 cytochrome-c peroxidase

Inhibitors

Inhibitors on EC 1.11.1.5 - cytochrome-c peroxidase

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-heptyl-4-hydroxyquinoline N-oxide
-
-
3-Amino-1,2,4-triazole
-
2 mM, in the presence of 2 mM H2O2, noticeably retards the growth of the enzyme gene disrupted mutants
Ag+
-
inhibition of NADH oxidizing activity
azide
Ca2+
-
1 mM of the cation in the assay solution inhibits the oxidation of horse cytochrome c but not Pseudomonas stutzeri cytochrome c551
Cu2+
-
inhibition of NADH oxidizing activity
cyanide
cytochrome c551
-
above 0.05 mM, substrate inhibition
-
Hg2+
-
inhibition of NADH oxidizing activity
L-ascorbate
nitric oxide
-
complete suppression of activity. Nitrosyl complexes of cytochrome c produced during inhibition are sensitive to laser irradiation and are photolyzed during irradiation. Decomposition leads to partial restoration of enzyme activity
nitrite
-
2 mM, in the presence of 0.88 M of H2O2, inhibits 50% enzyme activity
Pb2+
-
inhibition of NADH oxidizing activity
additional information
-
mixed-monolayer protected colloids selectively interact with enzyme and cytochrome c based upon charge complementarity. Surface-functionalized colloids with gold cores and thiolates terminating in trimethyl-amine bind reversibly and proteins retain their native structure. Binding is reversed by high ionic strength
-