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
-
1.11.1.5
-
peroxidases
-
horseradish
-
horse
-
high-spin
-
paramagnetic
-
low-spin
-
ferrous
-
porphyrin
-
ferryl
-
peroxidatic
-
paracoccus
-
iso-1-cytochrome
-
soret
-
electron-transfer
-
ferricytochrome
-
kraut
-
denitrificans
-
ccp1
-
hexacoordinate
-
oxyferryl
-
katgs
-
catalase-peroxidase
-
poulos
-
pentacoordinate
-
chrysosporium
-
interprotein
-
intracomplex
-
five-coordinate
-
high-potential
-
ferrocyanide
-
phanerochaete
-
low-potential
-
six-coordinate
-
azurin
-
pi-cation
-
chloroperoxidase
-
protoheme
-
5-coordinate
-
half-reduced
-
pantotrophus
-
nitrosomonas
-
hyperfine-shifted
-
metmyoglobins
-
biotechnology
- 1.11.1.5
- peroxidases
- horseradish
- horse
-
high-spin
-
paramagnetic
-
low-spin
-
ferrous
- porphyrin
-
ferryl
-
peroxidatic
- paracoccus
-
iso-1-cytochrome
-
soret
-
electron-transfer
- ferricytochrome
-
kraut
- denitrificans
- ccp1
-
hexacoordinate
-
oxyferryl
-
katgs
- catalase-peroxidase
-
poulos
-
pentacoordinate
- chrysosporium
-
interprotein
-
intracomplex
-
five-coordinate
-
high-potential
- ferrocyanide
-
phanerochaete
-
low-potential
-
six-coordinate
- azurin
-
pi-cation
- chloroperoxidase
- protoheme
-
5-coordinate
-
half-reduced
- pantotrophus
- nitrosomonas
-
hyperfine-shifted
- metmyoglobins
- biotechnology
Reaction
2 ferrocytochrome c
+
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
1.11.1.5 cytochrome-c peroxidaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 1.11.1.5 - cytochrome-c peroxidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
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
Ca2+
-
1 mM of the cation in the assay solution inhibits the oxidation of horse cytochrome c but not Pseudomonas stutzeri cytochrome c551
cytochrome c551
-
above 0.05 mM, substrate inhibition
-
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
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
-
azide
mixed-type inhibition. Inhibitor binding occurs at the low-potential heme active site, shifting the resulting catalytic midpoint potential in a negative direction
cyanide
competitive. Inhibitor binding occurs at the low-potential heme active site, shifting the resulting catalytic midpoint potential in a negative direction
cyanide
-
the W51H mutations have a weaker effect on cyanide binding, with the cyanide affinity only 2-8times weaker than for cytochrome c peroxidase. The cyanide association rate constants are between 5 and 85times slower for the W51H mutants, while the cyanide dissociation rate constants range from 3times slower to 6times faster than those of wild-type cytochrome c peroxidase
cyanide
-
cyanide binding can act as a surrogate for the hydrogen peroxide reaction. Structural features that are important for accelerating cyanide binding are also important for accelerating the rate of hydrogen peroxide binding to the heme iron, equilibrium dissociation constants of wild-type and mutant enzymes, and pH-independent equilibrium dissociation constants for the high- and low-affinity cyanide binding phases of the triple mutants, overview
H2O2
at a concentration of 8% and 16% can inhibit the growth of wild-type strain H99
H2O2
-
2 mM, noticeably retards the growth of the enzyme gene disrupted mutants
L-ascorbate
-
poising the enzyme in the active state using sodium L-ascorbate, allows for capturing a highly active state that turns over peroxide in a high potential regime
L-ascorbate
poising the enzyme in the active state using sodium L-ascorbate, allows for capturing a highly active state that turns over peroxide in a high potential regime
