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
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high-spin
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paramagnetic
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low-spin
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ferrous
- porphyrin
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ferryl
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peroxidatic
- paracoccus
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iso-1-cytochrome
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soret
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electron-transfer
- ferricytochrome
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kraut
- denitrificans
- ccp1
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hexacoordinate
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oxyferryl
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katgs
- catalase-peroxidase
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poulos
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pentacoordinate
- chrysosporium
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interprotein
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intracomplex
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five-coordinate
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high-potential
- ferrocyanide
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phanerochaete
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low-potential
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six-coordinate
- azurin
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pi-cation
- chloroperoxidase
- protoheme
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5-coordinate
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half-reduced
- pantotrophus
- nitrosomonas
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hyperfine-shifted
- metmyoglobins
- biotechnology
Reaction
2 ferrocytochrome c
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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 (Engineering
Engineering on EC 1.11.1.5 - cytochrome-c peroxidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A124K/K128A
site-directed mutagenesis, no significant changes
G94K/K97Q/R100I
site-directed mutagenesis, triple point mutant is created to mimic the critical loop region of, but its crystal structure reveals that the inactive, bishistidinyl-coordinated form of the active-site heme group is retained
S134P
site-directed mutagenesis, distortion of the loop region, accompanied by an opening of the active-site loop, leaving the enzyme in a constitutively active state
S134P/V135K
site-directed mutagenesis, distortion of the loop region, accompanied by an opening of the active-site loop, leaving the enzyme in a constitutively active state
D37E/P44D/V45D
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redesign of a manganese-binding site, ratio kcat/KM values for manganese oxidation is 0.33 per mM and s at pH 5.0
D37E/V45E/H181E
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redesign of a manganese-binding site, ratio kcat/KM values for manganese oxidation is 0.25 per mM and s at pH 5.0
G41E/V45E/H181D
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redesign of a manganese-binding site, ratio kcat/KM values for manganese oxidation is 0.10 per mM and s at pH 5.0
G41E/V45E/W51F/H181D/W191F
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redesign of a manganese-binding site, ratio kcat/KM values for manganese oxidation is 0.6 per mM and s at pH 5.0
H71G
H71G/W94A
W94A
H74M
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no enzymatic activity, reduced redox potential. The introduced methionine does not ligate the N-terminal heme
M278H
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no enzymatic activity, reduced redox potential. Mutant contains two low-potential hemes
W97A
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no enzymatic activity. W97 is the mediator of intramolecular electron transfer of the enzyme
W97F
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no enzymatic activity. W97 is the mediator of intramolecular electron transfer of the enzyme
A193F
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surface mutant, shift in reduction potential to -170 mV. Analysis of spectroscopic properties
A193W
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mutant designed to incorporate a Trp-based extension to move oxidizing equivalents from the heme to the protein surface. Mutant is able to oxidize veratryl alcohol substrate with turnover numbers greater than wild type
A193W/Y229W
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mutant designed to incorporate a Trp-based extension to move oxidizing equivalents from the heme to the protein surface. Mutant is able to oxidize veratryl alcohol substrate with turnover numbers greater than wild type, possibly using an electron hopping mechanism
D146N
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surface mutant, shift in reduction potential to -173 mV. Analysis of spectroscopic properties
D146N/D148N
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surface mutant, shift in reduction potential to -173 mV. Analysis of spectroscopic properties
D235A
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proximal pocket mutant, shift in reduction potential to -78 mV. Analysis of spectroscopic properties
D235E
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proximal pocket mutant, shift in reduction potential to -113 mV. Analysis of spectroscopic properties
D235N
D34K
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the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c
D34N
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surface mutant, shift in reduction potential to -175 mV. Analysis of spectroscopic properties
D37K
E118K
E290C
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formation of a covalent complex with cytochrome c mutant K79C, kinetic studies. Residual activity of complex is due to unreacted enzyme that copurifies with the complex. In the complex, the Pelletier-Kraut site is blocked which results in zero catalytic activity
E290K
E290N
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surface mutant, shift in reduction potential to -177 mV. Analysis of spectroscopic properties
E291Q
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surface mutant, shift in reduction potential to -162 mV. Analysis of spectroscopic properties
E32Q
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surface mutant, shift in reduction potential to -168 mV. Analysis of spectroscopic properties
H52D
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distal pocket mutant, shift in reduction potential to -221 mV. Analysis of spectroscopic properties
H52E
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distal pocket mutant, reduction potential -183 mV, comparable to wild-type
H52K
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distal pocket mutant, shift in reduction potential to -157 mV. Analysis of spectroscopic properties
H52L
H52L/W191F
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proximal pocket mutant, shift in reduction potential to -151 mV. Analysis of spectroscopic properties
H52N |
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distal pocket mutant, shift in reduction potential to -259 mV, most negative reduction potential of all mutants analyzed. Analysis of spectroscopic properties
H52Q
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distal pocket mutant, shift in reduction potential to -224 mV. Analysis of spectroscopic properties
K12C
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characterization of complex with yeast cytochrome c mutant K79C. Cytochrome c is covalently bound and located 90° from its primary binding site. Catalytic activity is similar to wild-type cytochrome c peroxidase
K264C
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characterization of complex with yeast cytochrome c mutant K79C. Cytochrome c is covalently bound and located 90° from its primary binding site. Catalytic activity is similar to wild-type cytochrome c peroxidase
N184R
the N184R variant introduces potential hydrogen bonding interactions for ascorbate binding
N78C
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characterization of complex with yeast cytochrome c mutant K79C. Cytochrome c is covalently bound and located 90° from its primary binding site. Catalytic activity is similar to wild-type cytochrome c peroxidase
R48A/W51A/H52A
R48E
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distal pocket mutant, shift in reduction potential to -179 mV. Analysis of spectroscopic properties
R48K
R48L
R48L/W51L/H52L
R48L/W51L/H52L |
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site-directed mutagenesis, a distal pocket mutant
R48V/W51V/H52V
V197C/C128A
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as active as the wild-type enzyme. Used to generate a covalent complex with a mutant cytochrome c
V5C
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characterization of complex with yeast cytochrome c mutant K79C. Cytochrome c is covalently bound via disulfide formation of the mutated residues and located on the back-side of the enzyme, 180° from its primary binding site. Catalytic activity is similar to wild-type cytochrome c peroxidase. Significant electrostatic repulsion of the two cytochrome c molecules bound in an 2:1 complex which decreases as the ionic strength of buffer increases
W191F
W191G
provides a specific site near heme from which substrates might be oxidized
W51H
W51H/H52L
W51H/H52W
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altered electronic absorption spectra, indicating that the heme group in the mutants is six-coordinate rather than five-coordinate as it is in wild-type cytochrome c peroxidase, weaker effect on cyanide binding, with the cyanide affinity only 2-8times weaker than for cytochrome c peroxidase
Y229W
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mutant designed to incorporate a Trp-based extension to move oxidizing equivalents from the heme to the protein surface. Mutant is able to oxidize veratryl alcohol substrate with turnover numbers greater than wild type
Y36A
site-directed mutagenesis, Tyr36 directly blocks the equivalent ascorbate binding site in CcP and was therefore replaced with a less bulky residue
Y36A/N184R
site-directed mutagenesis, no significant spectroscopic changes on reaction with stoichiometric or higher amounts of H2O2 are seen
Y36A/N184R/W191F
site-directed mutagenesis, cytochrome c peroxidase enzyme can duplicate the substrate binding properties of ascorbate peroxidase through the introduction of relatively modest structural changes at Tyr36 and Asn184, no evidence for a porphyrin pi-cation radical
Y36A/W191F
site-directed mutagenesis, no significant spectroscopic changes on reaction with stoichiometric or higher amounts of H2O2 are seen
Y39A
site-directed mutagenesis, mutation has a destabilizing effect on binding
W191F
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catalytically inactive mature Ccp1 mutant, Ccp1W191F is a more persistent H2O2 signaling protein than wild-type Ccp1
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R48L/W51L/H52L |
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site-directed mutagenesis, a distal pocket mutant
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E123D
distal heme pocket mutant, no detectable electrocatalytic turnover of substrate in the highpotential regime
E123Q
distal heme pocket mutant, no detectable electrocatalytic turnover of substrate in the highpotential regime
F102W
distal heme pocket mutant, 10fold decrease in peroxidase activity and high-potential catalytic turnover of hydrogen peroxide
Q113N
distal heme pocket mutant, no detectable electrocatalytic turnover of substrate in the highpotential regime
W191F
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study of the role of intracomplex dynamics in controlling electron transfer, use of Zn-enzyme in 1:1 complex with cytochrome c
additional information
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
D235N
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proximal pocket mutant, shift in reduction potential to -79 mV. Analysis of spectroscopic properties
D37K
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the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c
E118K
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the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c
E290K
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the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c
H52L
exhibits multiple forms in solution, with a reversible temperature-dependent interconversion, indicating the presence of a dynamic equilibrium between enzyme forms, which favors an apparent single form at low temperature and low pH, and a different form at high temperature and high pH
H52L
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with slower cyanide dissociation rate constant for the heme group with respect to the wild-type enzyme
H52L
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distal pocket mutant, shift in reduction potential to -170 mV. Analysis of spectroscopic properties
R48A/W51A/H52A
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distal pocket mutant, shift in reduction potential to -163 mV. Analysis of spectroscopic properties
R48A/W51A/H52A
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site-directed mutagenesis, the mutant has altered pKA values compred to the wild-type enzyme
R48A/W51A/H52A
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site-directed mutagenesis, the mutant shows 34fold higher activity with 1-methoxynaphthalene than the wild-type enzyme. While wild-type CcP is very stable to oxidative degradation by excess hydrogen peroxide, mutant CcP is inactivated within four cycles of the peroxygenase reaction
R48A/W51A/H52A
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less than 0.02% of wild-type activity. The imidazole binding curve is biphasic. The fast phase of imidazole binding is linearly dependent on the imidazole concentration while the slow phase is independent of imidazole concentration. Imidazole binding is pH dependent with the strongest binding observed at high pH. Mutant displays higher binding affinities for 1-methylimidazole and 4-nitroimidazole than wild-type CcP
R48K
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distal pocket mutant, reduction potential -186 mV, comparable to wild-type. Analysis of spectroscopic properties
R48L
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distal pocket mutant, shift in reduction potential to -164 mV. Analysis of spectroscopic properties
R48L/W51L/H52L
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distal pocket mutant, shift in reduction potential to -146 mV. Analysis of spectroscopic properties
R48L/W51L/H52L
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site-directed mutagenesis, the mutant has altered pKA values compred to the wild-type enzyme
R48L/W51L/H52L
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site-directed mutagenesis, the mutant shows higher activity with 1-methoxynaphthalene than the wild-type enzyme
R48L/W51L/H52L
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less than 0.02% of wild-type activity. The imidazole binding curve is biphasic. The fast phase of imidazole binding is linearly dependent on the imidazole concentration while the slow phase is independent of imidazole concentration. Imidazole binding is pH dependent with the strongest binding observed at high pH. Mutant displays higher binding affinities for 1-methylimidazole and 4-nitroimidazole than wild-type CcP
R48V/W51V/H52V
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distal pocket mutant, shift in reduction potential to -150 mV. Analysis of spectroscopic properties
R48V/W51V/H52V
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site-directed mutagenesis, the mutant has altered pKA values compred to the wild-type enzyme
R48V/W51V/H52V
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site-directed mutagenesis, the mutant shows higher activity with 1-methoxynaphthalene than the wild-type enzyme
R48V/W51V/H52V
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less than 0.02% of wild-type activity. The imidazole binding curve is biphasic. Both phases have a hyperbolic dependence on the imidazole concentration. Imidazole binding is pH dependent with the strongest binding observed at high pH. Mutant displays higher binding affinities for 1-methylimidazole and 4-nitroimidazole than wild-type CcP
W191F
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proximal pocket mutant, shift in reduction potential to -202 mV. Analysis of spectroscopic properties
W191F
side chain replacement followed by four iterations of side chain sampling plus minimization of a region within 6 A of Trp191, in W191F partial formation of a covalent link from Trp51 to the heme is observed
W191F
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catalytically inactive mature Ccp1 mutant, Ccp1W191F is a more persistent H2O2 signaling protein than wild-type Ccp1
W191F
mutation eliminates electron fast hole hopping through residue W191, enhancing accumulation of charge-separated intermediate and extending the timescale for binding/dissociation of the charge-separated complex. The photocycle includes dissociation/recombination of the charge-separated binary complex and a charge-separated ternary complex, [Zn-protoporphyrin+CcP, Fe2+cytochrome c, Fe3+cytochrome]
W51H
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distal pocket mutant, shift in reduction potential to -200 mV. Analysis of spectroscopic properties
W51H
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altered electronic absorption spectra, indicating that the heme group in the mutants is six-coordinate rather than five-coordinate as it is in wild-type cytochrome c peroxidase, weaker effect on cyanide binding, with the cyanide affinity only 2-8times weaker than for cytochrome c peroxidase
W51H/H52L
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distal pocket mutant, shift in reduction potential to -162 mV. Analysis of spectroscopic properties
W51H/H52L
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altered electronic absorption spectra, indicating that the heme group in the mutants is six-coordinate rather than five-coordinate as it is in wild-type cytochrome c peroxidase, weaker effect on cyanide binding, with the cyanide affinity only 2-8times weaker than for cytochrome c peroxidase
additional information
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a mutant lacking the putative cytochrome c peroxidase DocA shows a 10fold reduction in colonization of the chick cecum compared to wild-type enzyme, a mutant lacking the putative cytochrome c peroxidase CJJ0382 demonstrates a maximal 50fold colonization defect that is dependent on the inoculum dose
additional information
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a mutant lacking the putative cytochrome c peroxidase DocA shows a 10fold reduction in colonization of the chick cecum compared to wild-type enzyme, a mutant lacking the putative cytochrome c peroxidase CJJ0382 demonstrates a maximal 50fold colonization defect that is dependent on the inoculum dose
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additional information
disruption and deletion mutants show intracellular growth defects in macrophage like cells in vitro. The enzyme provides protection against oxidative stress within macrophages in vitro
additional information
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disruption and deletion mutants show intracellular growth defects in macrophage like cells in vitro. The enzyme provides protection against oxidative stress within macrophages in vitro
additional information
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disruption and deletion mutants show intracellular growth defects in macrophage like cells in vitro. The enzyme provides protection against oxidative stress within macrophages in vitro
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additional information
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mutant with deletion of the translation start codon and 800 bp of the enzyme gene. Almost as active as the wild-type enzyme
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
additional information
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distal pocket mutants, proximal pocket mutants, channel mutants, surface mutations
additional information
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significant decreases in the rate of reaction with hydrogen peroxide with 56-, 300-, and 6200fold decreases for mutant (W51H), mutant (W51H/H52W), and mutant (W51H/H52L), respectively, compared to that of wild-type cytochrome c peroxidase, indicating that the position of the distal histidine has a significant effect on the rate of reaction with H2O2
additional information
variant of cytochrome c peroxidase in which the proposed electron transfer pathway is excised from the structure, leaving a water filled channel in its place
additional information
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construction of three apolar distal heme pocket mutants of CcP with altered pH dependencies compared to the wild-type enzyme
additional information
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construction of three apolar distal heme pocket mutants of CcP with enhanced binding of 1-methoxynaphthalene near the heme and enhanced hydroxylation activity of 1-methoxynaphthalene
additional information
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generation of enzyme disruption mutant DELTAccp1, SOD2 activity is significantly lower in W191F ccp1 mutant cells than in DELTAccp1 deletion mutant cells
additional information
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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
additional information
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generation of enzyme disruption mutant DELTAccp1, SOD2 activity is significantly lower in W191F ccp1 mutant cells than in DELTAccp1 deletion mutant cells
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additional information
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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
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additional information
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construction of a DELTAccpA mutant Shewanella oneidensis line
additional information
construction of disruption knockout mutant DELTAZmcytC, phenotype, overview
additional information
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construction of disruption knockout mutant DELTAZmcytC, phenotype, overview
