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Information on EC 1.11.1.5 - cytochrome-c peroxidase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P00431
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1.11.1.5 cytochrome-c peroxidaseIUBMB Comments
A hemoprotein.
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Word Map
- 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
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
apocytochrome c peroxidase
-
-
-
-
CCP
cytochrome c peroxidase
cytochrome c-551 peroxidase
-
-
-
-
cytochrome c-H2O oxidoreductase
-
-
-
-
cytochrome peroxidase
-
-
-
-
mesocytochrome c peroxidase azide
-
-
-
-
mesocytochrome c peroxidase cyanate
-
-
-
-
mesocytochrome c peroxidase cyanide
-
-
-
-
peroxidase, cytochrome c
-
-
-
-
CCP
-
-
-
-
cytochrome c peroxidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
kinetics, energy, catalysis information
-
2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
the enzyme uses hydrogen peroxide as an electron acceptor to oxidize cytochrome c. The enzyme is not essential for both cell viability and respiration. Its biological function is to reduce H2O2 generated during aerobic respiratory process. The enzyme may also act as a peroxynitrite scavenger
-
2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
only ferrocytochrome c bound at the Pelletier-Kraut site of enzyme is oxidized during turnover
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ferrocytochrome-c:hydrogen-peroxide oxidoreductase
A hemoprotein.
CAS REGISTRY NUMBER
COMMENTARY
9029-53-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
-
-
-
?
ferrocytochrome c + CN-
?
-
dominant binding pathway for H52L mutant, biphasic reaction
-
-
?
ferrocytochrome c + HCN
?
-
dominant binding pathway for wild-type enzyme
-
-
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
-
-
-
-
?
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
-
-
-
-
r
iso-1 ferrocytochrome c mutant C102T + H2O2
iso-1 ferricytochrome c mutant C102T + 2 H2O
-
-
-
-
?
yeast ferrocytochrome c + H2O2
yeast ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
via intermediate compound I formation. The rate-limiting step in CcP compound I formation is the binding of hydrogen peroxide to the heme iron rather than the redox chemistry involved in compound I formation
-
-
?
cytochrome c + H2O2
?
-
the reaction with hydrogen peroxide of the W51H/H52L mutant is much slower compared to those of the mutant W51H and W51H/H52W
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
H2O2 can be substituted by ethyl peroxide
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
horse heart
-
-
ir
additional information
?
-
investigation of the binding hot-spot residue Y39 in the weak protein complex of physiological redox partners yeast iso-1-cytochrome c and cytochrome c peroxidase, cytochrome c and cytochrome c peroxidase binding parameters
-
-
?
additional information
?
-
-
investigation of the binding hot-spot residue Y39 in the weak protein complex of physiological redox partners yeast iso-1-cytochrome c and cytochrome c peroxidase, cytochrome c and cytochrome c peroxidase binding parameters
-
-
?
additional information
?
-
formation of a covalent link from Trp51 to the heme on reaction with H2O2
-
-
?
additional information
?
-
investigation of an engineered channel mutant with the surrogate peptide (N-benzimidazole-propionic acid)-Gly-Ala-Ala (BzGAA), complete loss of functional activity in the BzGAA/ET channel mutant strongly supports proposals that the Trp-191 radical intermediate is required for efficient turnover of cyt c via the proposed ET pathway
-
-
?
additional information
?
-
-
no oxidation of ferrocytochrome c of bacteria, no mammalian ferrocytochrome b, b5, c1
-
-
?
additional information
?
-
-
Ccp1 functions as a terminal electron acceptor for sulfhydryl oxidase Erv1
-
-
?
additional information
?
-
-
residues Tyr71 and Tyr236 contribute primarily to the EPR spectrum of the tyrosyl radical. The heme distal-side Trp51 is involved in the intramolecular electron transfer between Tyr71 and the heme and formation of Tyr71 and Tyr236 radicals is independent of the [Fe(IV)=O Trp191+] radical intermediate. Tyr71 radical is the reactive species with the guaiacol substrate. Surface-exposed residue Tyr236 is the other radical site
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
?
additional information
?
-
investigation of the binding hot-spot residue Y39 in the weak protein complex of physiological redox partners yeast iso-1-cytochrome c and cytochrome c peroxidase, cytochrome c and cytochrome c peroxidase binding parameters
-
-
?
additional information
?
-
-
investigation of the binding hot-spot residue Y39 in the weak protein complex of physiological redox partners yeast iso-1-cytochrome c and cytochrome c peroxidase, cytochrome c and cytochrome c peroxidase binding parameters
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome c
-
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
-
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
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
H2O2
-
2 mM, noticeably retards the growth of the enzyme gene disrupted mutants
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
-
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
steady-state and transient kinetics, stopped-flow kinetics at pH 4.0 and pH 8.0 at 0.10 M ionic strength, 25 °C
-
0.71
ascorbate
wild-type cytochrome c peroxidase, pH 6.0, 25°C
93
cytochrome c
wild-type cytochrome c peroxidase, pH 6.0, 25°C
100
cytochrome c
mutant W191F, pH 6.0, 25°C, the W191F mutation dramatically reduces the activity toward cytochrome c, but in the other variants which do not contain the W191F mutation the activity toward cytochrome c is largely unaffected
14
guaiacol
mutant Y36A/N184R/W191F, pH 6.0, 25°C, guaiacol oxidation is not significantly affected by any of the mutations, including W191F, which is consistent with the idea that aromatic substrates such as guaiacol bind at a separate location close to the delta-heme edge and is clearly indicative of a different electron transfer pathway for the oxidation of these types of aromatic substrate
0.002
ferrocytochrome c
-
recombinant wild-type, pH 7.5, 25°C, 100 mM phosphate buffer
0.0041
ferrocytochrome c
-
horse heart, with electron acceptor ethyl peroxide
0.011
ferrocytochrome c
-
covalent complex of mutant E290C, pH 7.5, 25°C, 100 mM phosphate buffer. Activity is due to unreacted enzyme copurifying with the complex
0.023
ferrocytochrome c
-
yeast, with electron acceptor ethyl peroxide
0.047
ferrocytochrome c
-
recombinant wild-type, pH 7.5, 25°C, 10 mM phosphate buffer
0.13
ferrocytochrome c
-
covalent complex of mutant E290C, pH 7.5, 25°C, 10 mM phosphate buffer. Activity is due to unreacted enzyme copurifying with the complex
0.0019
iso-1 ferrocytochrome c
-
mutant enzyme D210K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.002
iso-1 ferrocytochrome c
-
mutant enzyme D18K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0021
iso-1 ferrocytochrome c
-
recombinant wild type enzyme, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0023
iso-1 ferrocytochrome c
-
mutant enzyme E17K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0024
iso-1 ferrocytochrome c
-
mutant enzyme D33K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0028
iso-1 ferrocytochrome c
-
mutant enzyme E209K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0029
iso-1 ferrocytochrome c
-
mutant enzyme E201K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0031
iso-1 ferrocytochrome c
-
mutant enzyme E98K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0035
iso-1 ferrocytochrome c
-
mutant enzyme E35K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0038
iso-1 ferrocytochrome c
-
mutant enzyme E291K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0045
iso-1 ferrocytochrome c
-
mutant enzyme E32K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.051
iso-1 ferrocytochrome c
-
mutant enzyme E118K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.06
iso-1 ferrocytochrome c
-
mutant enzyme E290K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.082
iso-1 ferrocytochrome c
-
mutant enzyme D37K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.1
iso-1 ferrocytochrome c
-
Km above 0.1 mM, mutant enzyme D34K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.1
iso-1 ferrocytochrome c
-
Km above 0.1 mM, mutant enzyme R31E, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.83
ascorbate
wild-type cytochrome c peroxidase, pH 6.0, 25°C
1510
cytochrome c
wild-type cytochrome c peroxidase, pH 6.0, 25°C
4.2
horse heart ferrocytochrome c
-
pH 6, 200 mM potassium phosphate, covalent complex
-
20.7
horse heart ferrocytochrome c
-
pH 6, 20 mM potassium phosphate, covalent complex
-
166.8
horse heart ferrocytochrome c
-
pH 6, 200 mM potassium phosphate, V197C/C128A mutant
-
175.1
horse heart ferrocytochrome c
-
pH 6, 200 mM potassium phosphate, wild-type enzyme
-
803.4
horse heart ferrocytochrome c
-
pH 6, 20 mM potassium phosphate, V197C/C128A mutant
-
850.3
horse heart ferrocytochrome c
-
pH 6, 20 mM potassium phosphate, wild-type enzyme
-
15.7
yeast ferrocytochrome c
-
pH 6, 20 mM potassium phosphate, covalent complex
-
76.2
yeast ferrocytochrome c
-
pH 6, 200 mM potassium phosphate, covalent complex
-
219.1
yeast ferrocytochrome c
-
pH 6, 20 mM potassium phosphate, wild-type enzyme
-
240.9
yeast ferrocytochrome c
-
pH 6, 20 mM potassium phosphate, V197C/C128A mutant
-
1167
yeast ferrocytochrome c
-
pH 6, 200 mM potassium phosphate, V197C/C128A mutant
-
1362
yeast ferrocytochrome c
-
pH 6, 200 mM potassium phosphate, wild-type enzyme
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8.6
-
the association rate constant for the binding of cyanide to H52L mutant varies almost 4 orders of magnitude in this pH range. Above pH 8 cyanide binds more rapidly to H52L mutant than to wild-type enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
malfunction
-
significantly higher H2O2 accumulation in ccp1-null cells and catalytically inactive Ccp1W191F mutant cells. Ccp1W191F is a more persistent H2O2 signaling protein than wild-type Ccp1
malfunction
-
while the wild-type CcP is very stable to oxidative degradation by excess hydrogen peroxide, CcP mutant R48A/W51A/H52A is inactivated within four cycles of the peroxygenase reaction
physiological function
-
CcP catalyzes reduction of hydroperoxides using the electrons provided by its physiological binding partner cytochrome c
physiological function
-
cytochrome c peroxidase is a mitochondrial heme-based H2O2 sensor that modulates antioxidant defense. The enzyme in intermembrane space functions primarily as a mitochondrial H2O2 sensing and signaling protein in yeast cells. Ccp1 H2O2 sensing and signaling regulate Sod2 activity to control superoxide levels. Respiration-derived H2O2 is removed principally by mitochondrial catalase Cta1, which is regulated in a H2O2-dependent manner by Ccp1, overview
physiological function
-
increased copy number of CCP1 on chromosome XI activates respiratory metabolism and decreases pyruvate levels in an aneuploid sake yeast
additional information
-
His175 and Asp235 in the proximal heme pocket form another H-bonding cluster that provides a proton-binding site that is responsive to changes in the redox state of the heme iron. Arg-48 is not a good candidate for the proton-binding site. Arg48 interacts with multiple waters, is located near the bottom of the solvent-access channel in CcP. The carboxylate group of heme propionate-7, His181, and Asp37 form a hydrogen-bonded cluster near the heme iron
additional information
-
resting ferric (FeIII) Ccp1III is oxidized by H2O2 to compound I,which has a FeIV heme and a cation radical on residue W191. Compound I reacts with ferrous (FeII) Cyc1II to form compound II with a FeIV heme but no W191 radical. Reaction with a second Cyc1II reduces the FeIV heme to yield resting Ccp1III. The Ccp1W191F variant rapidly reacts with H2O2 but is very slowly reduced by Cyc1II such that it exhibits negligible Cyc1II-oxidizing activity, reaction mechanism, overview
additional information
-
structural features that are important for accelerating cyanide binding are also important for accelerating the rate of hydrogen peroxide binding to the heme iron
additional information
-
the catalytic mechanism of H2O2 reduction involves formation of CcP Compound I (CpdI), an intermediate oxidized 2 equiv above the CcP Fe(III) resting state and containing Fe(IV)=O heme oxyferryl and W191 cation radical. Subsequent CpdI reduction occurs in two one-electron steps, involving complex formation with ferrous Cc, intermolecular electron transfer (ET), and product dissociation
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34100 - 35240
additional information
mutant W191F molecular weight 34196 Da after treatment with H2O2, covalent attachment of the heme (617 Da) to the apoenzyme (33561 Da)
34100 - 35240
-
amino acid sequence of apoprotein: 33419, of holoenzyme: 34036
34100 - 35240
-
sedimentation and diffusion constants, partial specific volume
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
recombinant His-tagged enzyme is used for structure analysis by multidimensional NMR spectroscopy, structure modeling, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
microdialysis, in 500 mM potassium phosphate, pH 6.0, against 50 mM potassium phosphate, pH 6.0, containing 30% 2-methyl-2,4-pentanediol
protein channel mutant with surrogate protein (N-benzimidazole-propionic acid)-Gly-Ala-Ala (BzGAA), vapor diffusion, 200 mM KPi, 25% MPD, pH 6.0, temperature 282K, space group P212121, resolution 1.6 A
structures for mutants N184R, Y36A, W191F, N184R/W191F, Y36A/W191, FY36A/N184R, Y36A/N184R/W191F, Y36A/N184R/W191F-ascorbate complex, no major perturbations compared to the wild type protein
apo and holo CcP exhibit very similar structural, hydrodynamic, and thermodynamic properties. Apo CcP is more expanded in solution, displays a number of characteristics associated with a molten globule state, and does not form an unfolding intermediate during thermal and chemical denaturation
-
of iron-free enzyme, removal of iron has no effect on porphyrin geometry and distortion, indicating that iron coordination is not responsible for prophyrin conformation. Iron depletion leads to changes in solvent structure in the distal pocket which result in changes in the distal H52 acid-base catalyst
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
N184R
the N184R variant introduces potential hydrogen bonding interactions for ascorbate binding
W191F
W191G
provides a specific site near heme from which substrates might be oxidized
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
A193F
-
surface mutant, shift in reduction potential to -170 mV. Analysis of spectroscopic properties
A193W
-
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
-
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
-
surface mutant, shift in reduction potential to -173 mV. Analysis of spectroscopic properties
D146N/D148N
-
surface mutant, shift in reduction potential to -173 mV. Analysis of spectroscopic properties
D235A
-
proximal pocket mutant, shift in reduction potential to -78 mV. Analysis of spectroscopic properties
D235E
-
proximal pocket mutant, shift in reduction potential to -113 mV. Analysis of spectroscopic properties
D235N
D34K
-
the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c
D34N
-
surface mutant, shift in reduction potential to -175 mV. Analysis of spectroscopic properties
D37K
E118K
E290C
-
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
-
surface mutant, shift in reduction potential to -177 mV. Analysis of spectroscopic properties
E291Q
-
surface mutant, shift in reduction potential to -162 mV. Analysis of spectroscopic properties
E32Q
-
surface mutant, shift in reduction potential to -168 mV. Analysis of spectroscopic properties
H52D
-
distal pocket mutant, shift in reduction potential to -221 mV. Analysis of spectroscopic properties
H52E
-
distal pocket mutant, reduction potential -183 mV, comparable to wild-type
H52K
-
distal pocket mutant, shift in reduction potential to -157 mV. Analysis of spectroscopic properties
H52L
H52L/W191F
-
proximal pocket mutant, shift in reduction potential to -151 mV. Analysis of spectroscopic properties
H52N |
-
distal pocket mutant, shift in reduction potential to -259 mV, most negative reduction potential of all mutants analyzed. Analysis of spectroscopic properties
H52Q
-
distal pocket mutant, shift in reduction potential to -224 mV. Analysis of spectroscopic properties
K12C
-
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
-
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
N78C
-
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
-
distal pocket mutant, shift in reduction potential to -179 mV. Analysis of spectroscopic properties
R48K
R48L
R48L/W51L/H52L
R48L/W51L/H52L |
-
site-directed mutagenesis, a distal pocket mutant
R48V/W51V/H52V
V197C/C128A
-
as active as the wild-type enzyme. Used to generate a covalent complex with a mutant cytochrome c
V5C
-
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
W51H
W51H/H52L
W51H/H52W
-
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
-
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
additional information
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
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]
D235N
-
proximal pocket mutant, shift in reduction potential to -79 mV. Analysis of spectroscopic properties
D37K
-
the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c
E118K
-
the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c
E290K
-
the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c
H52L
-
with slower cyanide dissociation rate constant for the heme group with respect to the wild-type enzyme
H52L
-
distal pocket mutant, shift in reduction potential to -170 mV. Analysis of spectroscopic properties
R48A/W51A/H52A
-
distal pocket mutant, shift in reduction potential to -163 mV. Analysis of spectroscopic properties
R48A/W51A/H52A
-
site-directed mutagenesis, the mutant has altered pKA values compred to the wild-type enzyme
R48A/W51A/H52A
-
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
-
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
-
distal pocket mutant, reduction potential -186 mV, comparable to wild-type. Analysis of spectroscopic properties
R48L
-
distal pocket mutant, shift in reduction potential to -164 mV. Analysis of spectroscopic properties
R48L/W51L/H52L
-
distal pocket mutant, shift in reduction potential to -146 mV. Analysis of spectroscopic properties
R48L/W51L/H52L
-
site-directed mutagenesis, the mutant has altered pKA values compred to the wild-type enzyme
R48L/W51L/H52L
-
site-directed mutagenesis, the mutant shows higher activity with 1-methoxynaphthalene than the wild-type enzyme
R48L/W51L/H52L
-
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
-
distal pocket mutant, shift in reduction potential to -150 mV. Analysis of spectroscopic properties
R48V/W51V/H52V
-
site-directed mutagenesis, the mutant has altered pKA values compred to the wild-type enzyme
R48V/W51V/H52V
-
site-directed mutagenesis, the mutant shows higher activity with 1-methoxynaphthalene than the wild-type enzyme
R48V/W51V/H52V
-
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
-
proximal pocket mutant, shift in reduction potential to -202 mV. Analysis of spectroscopic properties
W191F
-
catalytically inactive mature Ccp1 mutant, Ccp1W191F is a more persistent H2O2 signaling protein than wild-type Ccp1
W51H
-
distal pocket mutant, shift in reduction potential to -200 mV. Analysis of spectroscopic properties
W51H
-
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
-
distal pocket mutant, shift in reduction potential to -162 mV. Analysis of spectroscopic properties
W51H/H52L
-
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
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
-
distal pocket mutants, proximal pocket mutants, channel mutants, surface mutations
additional information
-
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
-
construction of three apolar distal heme pocket mutants of CcP with altered pH dependencies compared to the wild-type enzyme
additional information
-
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
-
generation of enzyme disruption mutant DELTAccp1, SOD2 activity is significantly lower in W191F ccp1 mutant cells than in DELTAccp1 deletion mutant cells
additional information
-
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
-
mutants W51H, W51H/H52W and W51H/H52L are significantly less stable at pH 4.0 than wild-type cytochrome c peroxidase, at pH 4, the Soret band of the spectra for all three mutants undergoes a loss of absorptivity, suggesting the beginning of acid denaturation
702313
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
crystals stable in water-saturated atmosphere for more than 5 h at 23°C
-
in presence of guanidinium HCl, both apo and holo CcP exhibit single transitions, with midpoints of 1.34 M and 1.40 M for apo and holo CcP, rrespectively
-
in presence of urea, the transition midpoint is 4.12 M for apo CcP and 3.72 M for the holo protein
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
while the wild-type CcP is very stable to oxidative degradation by excess hydrogen peroxide, CcP mutant R48A/W51A/H52A is inactivated within four cycles of the peroxygenase reaction
-
724658
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
high-purity V197C/C128A mutant is obtained after an anion-exchange chromatography and gel filtration
-
recombinant soluble His-tagged Ccp from Escherichia coli strain BL21(DE3) by immobilized metal affinity chromatography and gel filtration
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by anion exchange chromatography and dialysis
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
functional expression of deuterated and soluble His-tagged Ccp in Escherichia coli strain BL21(DE3). Introduction of a His-tag at either protein terminus dramatically increases its solubility, allowing preparation of concentrated, stable CcP samples. The engineered His tags neither perturb the structure of the enzyme nor alter the heme environment or its reactivity toward known ligands
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
cytochrome c peroxidase as a platform to develop specific peroxygenation catalysts
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Arch. Biochem. Biophys.
203
605-614
1980
Saccharomyces cerevisiae
Yonetani, T.
Cytochrome C peroxidase
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345-361
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Saccharomyces cerevisiae, Saccharomyces pastorianus
-
Yonetani, T.; Chance, B.; Kajiwara, S.
Crystalline cytochrome c peroxidase and complex ES
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Saccharomyces cerevisiae
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1965
Saccharomyces cerevisiae
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Cytochrome c peroxidase. 2. The size and shape of cytochrome c peroxidase of bakers yeast
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1967
Saccharomyces cerevisiae
Yonetani, T.
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Saccharomyces cerevisiae
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Primary structure of yeast cytochrome c peroxidase. II. The complete amino acid sequence
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203
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Saccharomyces cerevisiae
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Affinity chromatography purification of cytochrome c binding enzymes
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Saccharomyces cerevisiae
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Crystal structure of nitric oxide inhibited cytochrome c peroxidase
Biochemistry
27
8074-8081
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Saccharomyces cerevisiae
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The crystal structure of fluoride-inhibited cytochrome c peroxidase
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Saccharomyces cerevisiae
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Saccharomyces cerevisiae
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Introduction of novel substrate oxidation into cytochrome c peroxidase by cavity complementation: Oxidation of 2-aminothiazole and covalent modification of the enzyme
Biochemistry
36
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1997
Saccharomyces cerevisiae (P00431)
Vitello, L.B.; Erman, J.E.; Miller, M.A.; Wang, J.; Kraut, J.
Effect of arginine-48 replacement on the reaction between cytochrome c peroxidase and hydrogen peroxide
Biochemistry
32
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Saccharomyces cerevisiae
Erman, J.E.; Vitello, L.B.
Cytochrome c peroxidase: a model heme protein
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31
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Saccharomyces cerevisiae
-
Erman, J.E.; Vitello, L.B.
Yeast cytochrome c peroxidase: mechanistic studies via protein engineering
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2002
Saccharomyces cerevisiae
Savenkova, M.I.; Satterlee, J.D.; Erman, J.E.; Siems, W.F.; Helms, G.L.
Expression, purification, characterization, and NMR studies of highly deuterated recombinant cytochrome c peroxidase
Biochemistry
40
12123-12131
2001
Saccharomyces cerevisiae (P00431), Saccharomyces cerevisiae
Bidwai, A.; Witt, M.; Foshay, M.; Vitello, L.B.; Satterlee, J.D.; Erman, J.E.
Cyanide binding to cytochrome c peroxidase (H52L)
Biochemistry
42
10764-10771
2003
Saccharomyces cerevisiae
Satterlee, J.D.; Savenkova, M.I.; Foshay, M.; Erman, J.E.
Temperature, pH, and solvent isotope dependent properties of the active sites of resting-state and cyanide-ligated recombinant cytochrome c peroxidase (H52L) revealed by proton hyperfine resonance spectra
Biochemistry
42
10772-10782
2003
Saccharomyces cerevisiae (P00431)
Bonagura, C.A.; Bhaskar, B.; Shimizu, H.; Li, H.; Sundaramoorthy, M.; McRee, D.E.; Goodin, D.B.; Poulos, T.L.
High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase
Biochemistry
42
5600-5608
2003
Saccharomyces cerevisiae
Kwon, M.; Chong, S.; Han, S.; Kim, K.
Oxidative stresses elevate the expression of cytochrome c peroxidase in Saccharomyces cerevisiae
Biochim. Biophys. Acta
1623
1-5
2003
Saccharomyces cerevisiae
Guo, M.; Bhaskar, B.; Li, H.; Barrows, T.P.; Poulos, T.L.
Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link
Proc. Natl. Acad. Sci. USA
101
5940-5945
2004
Saccharomyces cerevisiae
Nakani, S.; Vitello, L.B.; Erman, J.E.
Characterization of four covalently-linked yeast cytochrome c/cytochrome c peroxidase complexes: Evidence for electrostatic interaction between bound cytochrome c molecules
Biochemistry
45
14371-14378
2006
Saccharomyces cerevisiae
Nakani, S.; Viriyakul, T.; Mitchell, R.; Vitello, L.B.; Erman, J.E.
Characterization of a covalently linked yeast cytochrome c-cytochrome c peroxidase complex: evidence for a single, catalytically active cytochrome c binding site on cytochrome c peroxidase
Biochemistry
45
9887-9893
2006
Saccharomyces cerevisiae
Bayraktar, H.; Ghosh, P.S.; Rotello, V.M.; Knapp, M.J.
Disruption of protein-protein interactions using nanoparticles: inhibition of cytochrome c peroxidase
Chem. Commun. (Camb. )
2006
1390-1392
2006
Saccharomyces cerevisiae
Bhaskar, B.; Poulos, T.L.
The 1.13-A structure of iron-free cytochrome c peroxidase
J. Biol. Inorg. Chem.
10
425-430
2005
Saccharomyces cerevisiae
Dicarlo, C.M.; Vitello, L.B.; Erman, J.E.
Effect of active site and surface mutations on the reduction potential of yeast cytochrome c peroxidase and spectroscopic properties of the oxidized and reduced enzyme
J. Inorg. Biochem.
101
603-613
2007
Saccharomyces cerevisiae
Pearl, N.M.; Jacobson, T.; Arisa, M.; Vitello, L.B.; Erman, J.E.
Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: mutations near the high-affinity cytochrome c binding site
Biochemistry
46
8263-8272
2007
Saccharomyces cerevisiae
Pearl, N.M.; Jacobson, T.; Meyen, C.; Clementz, A.G.; Ok, E.Y.; Choi, E.; Wilson, K.; Vitello, L.B.; Erman, J.E.
Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: evidence for a single, catalytically active, cytochrome c binding domain
Biochemistry
47
2766-2775
2008
Saccharomyces cerevisiae
Dabir, D.V.; Leverich, E.P.; Kim, S.K.; Tsai, F.D.; Hirasawa, M.; Knaff, D.B.; Koehler, C.M.
A role for cytochrome c and cytochrome c peroxidase in electron shuttling from Erv1
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26
4801-4811
2007
Saccharomyces cerevisiae
Metcalfe, C.; Macdonald, I.K.; Murphy, E.J.; Brown, K.A.; Raven, E.L.; Moody, P.C.
The tuberculosis prodrug isoniazid bound to activating peroxidases
J. Biol. Chem.
283
6193-6200
2008
Saccharomyces cerevisiae (P00431)
Murphy, E.J.; Metcalfe, C.L.; Basran, J.; Moody, P.C.; Raven, E.L.
Engineering the substrate specificity and reactivity of a heme protein: creation of an ascorbate binding site in cytochrome c peroxidase
Biochemistry
47
13933-13941
2008
Saccharomyces cerevisiae (P00431)
Hays Putnam, A.M.; Lee, Y.T.; Goodin, D.B.
Replacement of an electron transfer pathway in cytochrome c peroxidase with a surrogate peptide
Biochemistry
48
1-3
2009
Saccharomyces cerevisiae (P00431)
Pipirou, Z.; Guallar, V.; Basran, J.; Metcalfe, C.L.; Murphy, E.J.; Bottrill, A.R.; Mistry, S.C.; Raven, E.L.
Peroxide-dependent formation of a covalent link between Trp51 and the heme in cytochrome c peroxidase
Biochemistry
48
3593-3599
2009
Saccharomyces cerevisiae (P00431)
Foshay, M.C.; Vitello, L.B.; Erman, J.E.
Relocation of the distal histidine in cytochrome c peroxidase: properties of CcP(W51H), CcP(W51H/H52W), and CcP(W51H/H52L)
Biochemistry
48
5417-5425
2009
Saccharomyces cerevisiae
Volkov, A.N.; Bashir, Q.; Worrall, J.A.; Ubbink, M.
Binding hot spot in the weak protein complex of physiological redox partners yeast cytochrome C and cytochrome C peroxidase
J. Mol. Biol.
385
1003-1013
2009
Saccharomyces cerevisiae (P00431), Saccharomyces cerevisiae
Meharenna, Y.T.; Doukov, T.; Li, H.; Soltis, S.M.; Poulos, T.L.
Crystallographic and single-crystal spectral analysis of the peroxidase ferryl intermediate
Biochemistry
49
2984-2986
2010
Saccharomyces cerevisiae (P00431)
Volkov, A.N.; Wohlkonig, A.; Soror, S.H.; van Nuland, N.A.
Expression, purification, characterization, and solution nuclear magnetic resonance study of highly deuterated yeast cytochrome C peroxidase with enhanced solubility
Biochemistry
52
2165-2175
2013
Saccharomyces cerevisiae
Bidwai, A.K.; Meyen, C.; Kilheeney, H.; Wroblewski, D.; Vitello, L.B.; Erman, J.E.
Apolar distal pocket mutants of yeast cytochrome c peroxidase: hydrogen peroxide reactivity and cyanide binding of the TriAla, TriVal, and TriLeu variants
Biochim. Biophys. Acta
1834
137-148
2013
Saccharomyces cerevisiae
Erman, J.E.; Kilheeney, H.; Bidwai, A.K.; Ayala, C.E.; Vitello, L.B.
Peroxygenase activity of cytochrome c peroxidase and three apolar distal heme pocket mutants: hydroxylation of 1-methoxynaphthalene
BMC Biochem.
14
19
2013
Saccharomyces cerevisiae
Martins, D.; Kathiresan, M.; English, A.M.
Cytochrome c peroxidase is a mitochondrial heme-based H2O2 sensor that modulates antioxidant defense
Free Radic. Biol. Med.
65C
541-551
2013
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
DiCarlo, C.M.; Vitello, L.B.; Erman, J.E.
Reduction potential of yeast cytochrome c peroxidase and three distal histidine mutants: dependence on pH
J. Inorg. Biochem.
105
532-537
2011
Saccharomyces cerevisiae, Saccharomyces cerevisiae Red Star
Chinchilla, D.; Kilheeney, H.; Vitello, L.; Erman, J.
Kinetic and equilibrium studies of acrylonitrile binding to cytochrome c peroxidase and oxidation of acrylonitrile by cytochrome c peroxidase compound I
Biochem. Biophys. Res. Commun.
443
200-204
2014
Saccharomyces cerevisiae
Miner, K.D.; Pfister, T.D.; Hosseinzadeh, P.; Karaduman, N.; Donald, L.J.; Loewen, P.C.; Lu, Y.; Ivancich, A.
Identifying the elusive sites of tyrosyl radicals in cytochrome c peroxidase implications for oxidation of substrates bound at a site remote from the heme
Biochemistry
53
3781-3789
2014
Saccharomyces cerevisiae
Sterckx, Y.G.; Volkov, A.N.
Cofactor-dependent structural and binding properties of yeast cytochrome C peroxidase
Biochemistry
53
4526-4536
2014
Saccharomyces cerevisiae
Page, T.R.; Hoffman, B.M.
Control of cyclic photoinitiated electron transfer between cytochrome c peroxidase (W191F) and cytochrome c by formation of dynamic binary and ternary complexes
Biochemistry
54
1188-1197
2015
Saccharomyces cerevisiae (P00431), Saccharomyces cerevisiae
Bidwai, A.; Ayala, C.; Vitello, L.B.; Erman, J.E.
Apolar distal pocket mutants of yeast cytochrome c peroxidase Binding of imidazole, 1-methylimidazole and 4-nitroimidazole to the triAla, triVal, and triLeu variants
Biochim. Biophys. Acta
1854
919-929
2015
Saccharomyces cerevisiae
Field, M.J.; Bains, R.K.; Warren, J.J.
Using an artificial tryptophan "wire" in cytochrome c peroxidase for oxidation of organic substrates
Dalton Trans.
46
11078-11083
2017
Saccharomyces cerevisiae
Schilder, J.; Loehr, F.; Schwalbe, H.; Ubbink, M.
The cytochrome c peroxidase and cytochrome c encounter complex the other side of the story
FEBS Lett.
588
1873-1878
2014
Saccharomyces cerevisiae (P00431)
van Son, M.; Schilder, J.T.; Di Savino, A.; Blok, A.; Ubbink, M.; Huber, M.
The transient complex of cytochrome c and cytochrome c peroxidase insights into the encounter complex from multifrequency EPR and NMR spectroscopy
Chemphyschem
21
1060-1069
2020
Saccharomyces cerevisiae (P00431), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P00431)
Fujimaru, Y.; Kusaba, Y.; Zhang, N.; Dai, H.; Yamamoto, Y.; Takasaki, M.; Kakeshita, T.; Kitagaki, H.
Extra copy of the mitochondrial cytochrome-c peroxidase gene confers a pyruvate-underproducing characteristic of sake yeast through respiratory metabolism
J. Biosci. Bioeng.
131
640-646
2021
Saccharomyces cerevisiae, Saccharomyces cerevisiae K7-4
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