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 + + 2 H+ = + 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
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Cofactor
Cofactor on EC 1.11.1.5 - cytochrome-c peroxidase
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holo CcP binds cytochrome c with micromolar affinity. For apo CcP, the interaction with cytochrome c is completely abolished
cytochrome c
study on both chemical shift perturbations and paramagnetic relaxation enhancements effects in the NMR spectrum of CcP generated in the presence of spin-labelled cytochrome c
cytochrome c
thermodynamic affinity constants for binding the first and second cytochrome c are KI 0.0000001 per M, KII 0.0001 per M. Cytochrome c binds at the weaker-binding site with relatively great affinity, and places upper bounds on the contributions of repulsion between the two cytochrome c of the ternary complex
heme
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Fe(III) reduction to Fe(IV) in heme cofactor, pH dependence of the reduction potential and heme binding site structure analysis of wild-type and mutant enzymes using photoreduction and spectroscopic methods, respectively, overview
heme
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diheme enzyme. L-heme is five-coordinate (5C) and (presumably) high-spin. H-heme is required for the L-heme to become 5C (no water or exogenous ligand bound)