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
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1.11.1.5
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peroxidases
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horseradish
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horse
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high-spin
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paramagnetic
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low-spin
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ferrous
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porphyrin
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ferryl
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peroxidatic
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paracoccus
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iso-1-cytochrome
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soret
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electron-transfer
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ferricytochrome
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kraut
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denitrificans
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ccp1
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hexacoordinate
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oxyferryl
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katgs
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catalase-peroxidase
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poulos
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pentacoordinate
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chrysosporium
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interprotein
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intracomplex
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five-coordinate
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high-potential
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ferrocyanide
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phanerochaete
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low-potential
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six-coordinate
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azurin
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pi-cation
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chloroperoxidase
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protoheme
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5-coordinate
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half-reduced
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pantotrophus
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nitrosomonas
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hyperfine-shifted
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metmyoglobins
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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
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RENATURED/Commentary 
ORGANISM
UNIPROT
LITERATURE
complete suppression of enzyme activity by niric oxide. 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. nitric oxide and laser irradiation may serve as instruments for regulating the peroxidase activity of cytochrome c and, probably, apoptosis
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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
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