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EC Tree
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa The enzyme appears in selected viruses and cellular organisms
Synonyms
cytochrome c peroxidase, cytochrome-c peroxidase, diheme cytochrome c peroxidase, cytochrome peroxidase, cjj0382, apocytochrome c peroxidase, cytochrome c-551 peroxidase, di-heme cytochrome c peroxidase,
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cytochrome c peroxidase
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apocytochrome c peroxidase
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cytochrome c-551 peroxidase
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cytochrome c-H2O oxidoreductase
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cytochrome peroxidase
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mesocytochrome c peroxidase azide
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mesocytochrome c peroxidase cyanate
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mesocytochrome c peroxidase cyanide
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peroxidase, cytochrome c
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CCP
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cytochrome c peroxidase
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cytochrome c peroxidase
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2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
reaction scheme
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ferrocytochrome-c:hydrogen-peroxide oxidoreductase
A hemoprotein.
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ferrocytochrome c + H2O2
ferricytochrome c + H2O
azurin + H2O2
oxidized azurin + ?
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blue copper protein
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?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
ferrocytochrome c551 + H2O2
ferricytochrome c551 + OH-
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?
reduced cytochrome c551 + H2O2
oxidized cytochrome c551 + H2O
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?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
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?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
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?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
investigation of the catalytic mechanism
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?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
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?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
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horse heart
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?
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ferrocytochrome c + H2O2
ferricytochrome c + H2O
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?
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Ca2+
a single, tightly bound, Ca2+ ion at the domain interface of both the fully oxidized and mixed-valence forms of the enzyme is absolutely required for catalytic activity, reduction of the electron-transferring (high-potential) heme in the presence of Ca2+ ions triggers substantial structural rearrangements around the active-site (low-potential) heme to allow substrate binding and catalysis
Fe
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static titration of ferric cytochrome c peroxidase with reduced azurin shows that only one of the two hemes in the enzyme seems to be readily reduced
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0.025
H2O2
protein film voltammetry, the midpoint potentials of the turnover signals are used to calculate Michaelis-Menten kinetics
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0.05
cyanide
pH 7, 25 microM H2O2, protein film voltammetry, the midpoint potentials of the turnover signals are used to calculate Michaelis-Menten kinetics
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3 - 10
by using the maximum current in the cathodic and anodic halfscans in the course of altering the pH a shift in potential is observed, at pH 7, a single redox couple (I) is dominant, but at more acidic pH values, a second couple (II) is clearly discernible at a more positive value of potential
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Uniprot
brenda
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36250
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electrospray mass spectrometry
36270
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MALDI-TOF mass spectrometry
44000
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amino acid analysis
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with 24% PEG 600, 0.2 M imidazole malate pH 5.5, 20 mM dithiothreitol
diffraction limit 2.5 A
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additional information
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an unactivated mutant devoid of the protein loop shows 10% of turnover activity of the wild type enzyme in the activated form
H71G
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about 55% of wild-type activity. Five-coordinate, peroxidatic heme structure contrary to six-coordinate structure of wild-type, formation of a tryptophan radical species during catalysis
H71G
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55% activity compared to the wild type enzyme, contains a high-spin, presumably five-coordinate, peroxidatic heme site
H71G
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the unactivated H71G mutant shows 75% of turnover activity of the wild-type enzyme in the activated form
H71G/W94A
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about 4% of wild-type activity. Five-coordinate, peroxidatic heme structure contrary to six-coordinate structure of wild-type, formation of a porphyrin radical species during catalysis
H71G/W94A
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4% activity compared to the wild type enzyme, contains a high-spin, presumably five-coordinate, peroxidatic heme site
W94A
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less than 1% of wild-type activity. Six-coordinate heme structure similar to wild-type
W94A
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less than 1% activity compared to the wild type enzyme, the mutant retains the normal six-coordinate heme structures
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3 - 10
by using the maximum current in the cathodic and anodic halfscans in the course of altering the pH a shift in potential is observed, at pH 7, a single redox couple (I) is dominant, but at more acidic pH values, a second couple (II) is clearly discernible at a more positive value of potential
702343
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unstable during degassing under vacuum except in presence of detergent
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precipitation, DEAE-Sepharose followed by S-100 size exclusion chromatography
S-Sepharose column chromatography and Superdex-75 gel filtration
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expressed in Escherichia coli JM109 (DE3) cells
expression in Escherichia coli JM109(DE3) with pETCCP coexpressed with pEC86
expressed in Escherichia coli JM109 (DE3) cells
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expression in Escherichia coli
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mutants expressed in Escherichia coli
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Ellfolk, N.; Rnnberg, M.; Aasa, R.; Andreasson, L.E.; Vnngard, T.
Properties and function of the two hemes in Pseudomonas cytochrome c peroxidase
Biochim. Biophys. Acta
743
23-30
1983
Pseudomonas aeruginosa
brenda
Foote, N.; Thompson, A.C.; Barber, D.; Greenwood, C.
Pseudomonas cytochrome C-551 peroxidase. A purification procedure and study of CO-binding kinetics
Biochem. J.
209
701-707
1983
Pseudomonas aeruginosa
brenda
Soininen, R.; Ellfolk, N.
Pseudomonas cytochrome c peroxidase. 8. The amino acid composition of the enzyme
Acta Chem. Scand.
27
2193-2198
1973
Pseudomonas aeruginosa
brenda
Samyn, B.; Van Craenenbroeck, K.; De Smet, L.; Vandenberghe, I.; Pettigrew, G.; Van Beeumen, J.
A reinvestigation of the covalent structure of Pseudomonas aeruginosa cytochrome c peroxidase
FEBS Lett.
377
145-149
1995
Pseudomonas aeruginosa
brenda
Ronnberg, M.; Araiso, T.; Ellfolk, N.; Dunford, H.B.
The reaction between reduced azurin and oxidized cytochrome c peroxidase from Pseudomonas aeruginosa
J. Biol. Chem.
256
2471-2474
1981
Pseudomonas aeruginosa
brenda
Fulop, V.; Little, R.
Crystallization and preliminary X-ray analysis of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa
J. Mol. Biol.
232
1208 - 1210
1993
Pseudomonas aeruginosa
brenda
Fulop, V.; Ridout, C.J.; Greenwood, C.; Hajdu, J.
Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa
Structure
3
1225-1233
1995
Pseudomonas aeruginosa
brenda
Lee, Y.; Boycheva, S.; Brittain, T.; Boyd, P.D.
Intramolecular electron transfer in the dihaem cytochrome c peroxidase of Pseudomonas aeruginosa
Chembiochem
8
1440-1446
2007
Pseudomonas aeruginosa
brenda
Echalier, A.; Brittain, T.; Wright, J.; Boycheva, S.; Mortuza, G.B.; Fueloep, V.; Watmough, N.J.
Redox-linked structural changes associated with the formation of a catalytically competent form of the diheme cytochrome c peroxidase from Pseudomonas aeruginosa
Biochemistry
47
1947-1956
2008
Pseudomonas aeruginosa (P14532), Pseudomonas aeruginosa
brenda
Hsiao, H.C.; Boycheva, S.; Watmough, N.J.; Brittain, T.
Activation of the cytochrome c peroxidase of Pseudomonas aeruginosa. The role of a heme-linked protein loop: a mutagenesis study
J. Inorg. Biochem.
101
1133-1139
2007
Pseudomonas aeruginosa
brenda
Becker, C.F.; Watmough, N.J.; Elliott, S.J.
Electrochemical evidence for multiple peroxidatic heme states of the diheme cytochrome c peroxidase of Pseudomonas aeruginosa
Biochemistry
48
87-95
2009
Pseudomonas aeruginosa (P14532), Pseudomonas aeruginosa
brenda