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1-methoxynaphthalene + H2O2
Russig's blue + 2 H2O
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
?
-
-
-
?
2,2'-azino-bis(3-ethylenbenzthiazoline-6-sulfonic acid) + H2O2
?
2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) + H2O2
?
-
-
-
-
?
2-aminothiazole + H2O2
?
modified enzyme
-
-
?
acrylonitrile + H2O2
? + H2O
-
-
-
-
?
ascorbate + H2O2
dehydroascorbate + H2O
azo violet + H2O2
? + H2O
-
-
-
-
?
azurin + H2O2
oxidized azurin + ?
brillant blue + H2O2
? + H2O
-
-
-
-
?
ferrocyanide + H2O2
ferricyanide + OH-
ferrocytochrome c + CN-
?
-
dominant binding pathway for H52L mutant, biphasic reaction
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + 2 H2O
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
ferrocytochrome c + HCN
?
-
dominant binding pathway for wild-type enzyme
-
-
?
ferrocytochrome c + menadione
ferricytochrome + oxidized menadione
-
menadione can be substituted by 1,4-naphthoquinone
-
-
?
ferrocytochrome c2 + H2O2
ferricytochrome c2 + OH-
-
-
-
-
?
ferrocytochrome c4 + H2O2
ferricytochrome c4 + OH-
-
-
-
?
ferrocytochrome c550 + H2O2
ferricytochrome c550 + H2O
-
-
-
-
r
ferrocytochrome c551 + H2O2
ferricytochrome c551 + OH-
ferrocytochrome c552 + H2O2
ferricytochrome c552 + OH-
ferrocytochrome c553 + H2O2
ferriytochrome c553 + OH-
-
-
-
-
?
ferrocytochrome c555 + H2O2
ferricytochrome c555 + OH-
-
-
-
-
?
ferrocytochrome c555 + H2O2
ferriytochrome c555 + OH-
-
-
-
-
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
horse ferrocytochrome c + H2O2
horse ferricytochrome c + H2O
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
hydroquinone + H2O2
benzoquinone + H2O
iso-1 ferrocytochrome c + H2O2
?
iso-1 ferrocytochrome c mutant C102T + H2O2
iso-1 ferricytochrome c mutant C102T + 2 H2O
-
-
-
-
?
iso-1-cytochrome c + ?
?
-
-
-
?
isoniazid + H2O2
?
-
-
-
?
NADH + H2O2
NAD+ + H2O
-
-
-
?
NADPH + H2O2
NADP+ + H2O
-
-
-
-
?
Reactive Black 5 + H2O2
? + H2O
-
-
-
-
?
reduced cytochrome c2 + H2O2
oxidized cytochrome c2 + H2O
reduced cytochrome c551 + H2O2
oxidized cytochrome c551 + H2O
-
-
-
-
?
reduced horse cytochrome c + H2O2
oxidized horse cytochrome c + H2O
reduced pseudoazurin + H2O2
oxidized pseudoazurin + H2O
-
-
-
-
?
Rhodobacter capsulatus ferrocytochrome c + H2O2
Rhodobacter capsulatus ferricytochrome c + H2O
Rhodobacter capsulatus ferrocytochrome c2 + H2O2
Rhodobacter capsulatus ferricytochrome c2 + H2O
veratryl alcohol + H2O2
veratraldehyde + H2O
-
-
-
-
?
yeast ferrocytochrome c + H2O2
yeast ferricytochrome c + H2O
-
-
-
-
r
additional information
?
-
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
activity with wild-type cytochrome c from Leishmania major and reduced activity with mutant cytochrome c R24A and K98A, no activity with cyt c mutant R24A/K98A
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 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
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
Marinobacter nauticus
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
Marinobacter nauticus 617
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
-
horse cytochrome c
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
-
Pseudomonas aeruginosa cytochrome c-551
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
-
Pseudomonas aeruginosa cytochrome c-551
-
-
?
2,2'-azino-bis(3-ethylenbenzthiazoline-6-sulfonic acid) + H2O2
?
-
-
-
?
2,2'-azino-bis(3-ethylenbenzthiazoline-6-sulfonic acid) + H2O2
?
-
-
-
?
ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
azurin + H2O2
oxidized azurin + ?
-
blue copper protein
-
-
?
azurin + H2O2
oxidized azurin + ?
-
blue copper protein
-
?
cytochrome c + H2O2
?
-
-
-
-
?
cytochrome c + H2O2
?
-
-
-
?
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
-
-
?
ferrocyanide + H2O2
ferricyanide + OH-
-
-
-
-
?
ferrocyanide + H2O2
ferricyanide + OH-
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
horse heart
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
antioxidant defense
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
antioxidant defense
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
horse heart
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
horse heart
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
investigation of the catalytic mechanism
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
horse heart
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
H2O2 can be substituted by ethyl peroxide
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
yeast
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
horse heart
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
H2O2 can be substituted by ethyl peroxide
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
yeast
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
horse heart
-
-
ir
ferrocytochrome c551 + H2O2
ferricytochrome c551 + OH-
-
-
-
?
ferrocytochrome c551 + H2O2
ferricytochrome c551 + OH-
-
-
-
?
ferrocytochrome c552 + H2O2
ferricytochrome c552 + OH-
Marinobacter nauticus
-
-
-
-
?
ferrocytochrome c552 + H2O2
ferricytochrome c552 + OH-
Marinobacter nauticus 617
-
-
-
-
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
-
-
-
-
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
-
-
-
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
-
-
-
-
?
horse ferrocytochrome c + H2O2
horse ferricytochrome c + H2O
-
-
-
-
r
horse ferrocytochrome c + H2O2
horse ferricytochrome c + H2O
-
-
-
-
r
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
-
-
-
-
?
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
-
-
-
-
?
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
-
-
-
-
?
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
-
-
-
-
r
hydroquinone + H2O2
benzoquinone + H2O
-
-
-
-
?
hydroquinone + H2O2
benzoquinone + H2O
-
-
-
-
?
iso-1 ferrocytochrome c + H2O2
?
-
-
-
-
?
iso-1 ferrocytochrome c + H2O2
?
-
C102T
-
-
?
pyrogallol + H2O2
?
-
-
-
-
?
pyrogallol + H2O2
?
-
-
-
-
?
reduced cytochrome c2 + H2O2
oxidized cytochrome c2 + H2O
-
-
-
-
?
reduced cytochrome c2 + H2O2
oxidized cytochrome c2 + H2O
-
-
-
-
?
reduced horse cytochrome c + H2O2
oxidized horse cytochrome c + H2O
-
-
-
-
?
reduced horse cytochrome c + H2O2
oxidized horse cytochrome c + H2O
-
-
-
-
?
Rhodobacter capsulatus ferrocytochrome c + H2O2
Rhodobacter capsulatus ferricytochrome c + H2O
-
-
-
-
r
Rhodobacter capsulatus ferrocytochrome c + H2O2
Rhodobacter capsulatus ferricytochrome c + H2O
-
-
-
-
r
Rhodobacter capsulatus ferrocytochrome c2 + H2O2
Rhodobacter capsulatus ferricytochrome c2 + H2O
-
-
-
-
r
Rhodobacter capsulatus ferrocytochrome c2 + H2O2
Rhodobacter capsulatus ferricytochrome c2 + H2O
-
-
-
-
r
additional information
?
-
-
Leishmania major peroxidase (LmP) exhibits both ascorbate and cytochrome c peroxidase activities, but cytochrome c is the natural substrate
-
-
?
additional information
?
-
-
Leishmania major cytochrome c has an electropositive surface surrounding the exposed heme edge that serves as the docking site with redox partners. Kinetic assays performed with Leishmania major cytochrome c and the enzyme show that it is a much better substrate for LmP than horse heart cytochrome c
-
-
?
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
?
-
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
?
-
-
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
-
-
?
additional information
?
-
-
no oxidation of ferrocytochrome c of bacteria, no mammalian ferrocytochrome b, b5, c1
-
-
?
additional information
?
-
-
menaquinol pool-based origin of electrons that are transferred to CcpA
-
-
?
additional information
?
-
the rate-limiting step involves a proton-coupled single electron reduction of a high valent iron species centered on the low-potential heme. Reduction shifts the pKa's of at least two amino acids. Loop 1 shifts during the rate-limiting step, changing the environment of residue His81
-
-
?
additional information
?
-
-
the rate-limiting step involves a proton-coupled single electron reduction of a high valent iron species centered on the low-potential heme. Reduction shifts the pKa's of at least two amino acids. Loop 1 shifts during the rate-limiting step, changing the environment of residue His81
-
-
?
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0.0113
2,2-azinobis(3-ethylbenzthiazolinesulfonic acid)
-
pH 7.5, temperature not specified in the publication
0.002 - 0.13
ferrocytochrome c
0.013
ferrocytochrome c550
-
-
-
510
ferrocytochrome c555
-
-
-
0.006
horse ferrocytochrome c
-
pH 7.0
-
0.042 - 0.066
horse heart ferrocytochrome c
-
0.0019 - 0.1
iso-1 ferrocytochrome c
-
0.06
Rhodobacter capsulatus ferrocyctochrome c
-
pH 7.0
-
additional information
additional information
-
0.31
ascorbate
mutant N184R/W191F, pH 6.0, 25°C
0.45
ascorbate
mutant W191, pH 6.0, 25°C
0.48
ascorbate
mutant FY36A/N184R, pH 6.0, 25°C
0.5
ascorbate
mutant Y36A/W191F, pH 6.0, 25°C
0.71
ascorbate
wild-type cytochrome c peroxidase, pH 6.0, 25°C
1.3
ascorbate
mutant Y36A/N184R/W191F, pH 6.0, 25°C
1.7
ascorbate
mutant N184R, pH 6.0, 25°C
1.7
ascorbate
mutant Y36A, 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
110
cytochrome c
mutant FY36A/N184R, pH 6.0, 25°C
140
cytochrome c
mutant N184R, pH 6.0, 25°C
160
cytochrome c
mutant Y36A/W191F, pH 6.0, 25°C
230
cytochrome c
mutant Y36A, pH 6.0, 25°C
300
cytochrome c
mutant Y36A/N184R/W191F, pH 6.0, 25°C
670
cytochrome c
mutant N184R/W191F, pH 6.0, 25°C
0.002
ferrocytochrome c
-
recombinant wild-type, pH 7.5, 25°C, 100 mM phosphate buffer
0.003
ferrocytochrome c
-
horse
0.0041
ferrocytochrome c
-
horse heart, with electron acceptor ethyl peroxide
0.0041
ferrocytochrome c
-
horse heart, with electron acceptor ethyl peroxide
0.0045
ferrocytochrome c
-
horse heart, with electron acceptor H2O2
0.0045
ferrocytochrome c
-
horse heart, with electron acceptor H2O2
0.005
ferrocytochrome c
-
horse heart
0.008
ferrocytochrome c
-
wild-type substrate, pH and temperature not specified in the publication
0.01
ferrocytochrome c
-
yeast
0.01
ferrocytochrome c
-
DELTA10 deltion mutant substrate, pH and temperature not specified in the publication
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
0.02
ferrocytochrome c
-
R24A substrate mutant, pH and temperature not specified in the publication
0.023
ferrocytochrome c
-
yeast, with electron acceptor ethyl peroxide
0.023
ferrocytochrome c
-
yeast, with electron acceptor ethyl peroxide
0.025
ferrocytochrome c
-
yeast, with electron acceptor H2O2
0.025
ferrocytochrome c
-
yeast, with electron acceptor H2O2
0.04
ferrocytochrome c
-
K98A substrate mutant, pH and temperature not specified in the publication
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
10
guaiacol
-
-
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
16
guaiacol
mutant FY36A/N184R, pH 6.0, 25°C
27
guaiacol
mutant N184R, pH 6.0, 25°C
34
guaiacol
mutant N184R/W191F, pH 6.0, 25°C
36
guaiacol
mutant Y36A, pH 6.0, 25°C
45
guaiacol
mutant Y36A/W191F, pH 6.0, 25°C
53
guaiacol
wild-type cytochrome c peroxidase, pH 6.0, 25°C
57
guaiacol
mutant W191, pH 6.0, 25°C
0.00013
H2O2
-
mutant F102W, pH 6.0, 23°C
0.0004
H2O2
-
mutant F81W, pH 6.0, 23°C
0.004
H2O2
mutant F102W, pH 6.0, 23°C
0.025
H2O2
protein film voltammetry, the midpoint potentials of the turnover signals are used to calculate Michaelis-Menten kinetics
0.042
horse heart ferrocytochrome c
-
bulk solution, 50 mM NaCl, at pH 7.0
-
0.066
horse heart ferrocytochrome c
-
membrane solution, 50 mM NaCl, at pH 7.0
-
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
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Rhodobacter capsulatus cytochrome c2 is slowly oxidized by peroxide in absence of presumed enzyme
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics with wild-type and mutant Leishmania major cytochrome c, overview. Comparison with kinetic of the enzyme from Saccharomyces cerevisiae
-
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
-
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0.00007 - 0.0025
1-methoxynaphthalene
23.1
2,2-azinobis(3-ethylbenzthiazolinesulfonic acid)
-
pH 7.5, temperature not specified in the publication
0.01
acrylonitrile
-
pH 6.0, 25°C
17.2 - 2000
ferrocytochrome c
17.7
ferrocytochrome c2
-
-
3.05
ferrocytochrome c555
-
-
-
40
horse ferrocytochrome c
-
pH 7.0
-
4.2 - 850.3
horse heart ferrocytochrome c
-
40
Rhodobacter capsulatus ferrocyctochrome c2
-
pH 7.0
-
15.7 - 1362
yeast ferrocytochrome c
-
additional information
additional information
-
0.00007
1-methoxynaphthalene
-
pH 7.0, 25°C, wild-type enzyme
0.0022
1-methoxynaphthalene
-
pH 7.0, 25°C, mutant R48L/W51L/H52L
0.0023
1-methoxynaphthalene
-
pH 7.0, 25°C, mutant R48V/W51V/H52V
0.0025
1-methoxynaphthalene
-
pH 7.0, 25°C, mutant R48A/W51A/H52A
0.25
ascorbate
mutant W191, pH 6.0, 25°C
0.27
ascorbate
mutant N184R/W191F, pH 6.0, 25°C
0.45
ascorbate
mutant Y36A/W191F, pH 6.0, 25°C
0.66
ascorbate
mutant FY36A/N184R, pH 6.0, 25°C
0.83
ascorbate
wild-type cytochrome c peroxidase, pH 6.0, 25°C
1.3
ascorbate
mutant Y36A, pH 6.0, 25°C
1.5
ascorbate
mutant N184R, pH 6.0, 25°C
2.6
ascorbate
mutant Y36A/N184R/W191F, pH 6.0, 25°C
0.06
cytochrome c
mutant Y36A/W191F, pH 6.0, 25°C
0.08
cytochrome c
mutant N184R/W191F, pH 6.0, 25°C
1.6
cytochrome c
mutant Y36A/N184R/W191F, pH 6.0, 25°C
1.7
cytochrome c
mutant W191, pH 6.0, 25°C
570
cytochrome c
mutant N184R, pH 6.0, 25°C
580
cytochrome c
mutant Y36A, pH 6.0, 25°C
600
cytochrome c
mutant FY36A/N184R, pH 6.0, 25°C
1510
cytochrome c
wild-type cytochrome c peroxidase, pH 6.0, 25°C
17.2
ferrocytochrome c
-
horse
23.6
ferrocytochrome c
-
horse
1500
ferrocytochrome c
-
yeast
2000
ferrocytochrome c
-
horse heart
0.9
guaiacol
mutant FY36A/N184R, pH 6.0, 25°C
1.5
guaiacol
mutant Y36A/N184R/W191F, pH 6.0, 25°C
3
guaiacol
mutant N184R, pH 6.0, 25°C
3.2
guaiacol
mutant Y36A/W191F, pH 6.0, 25°C
4.1
guaiacol
wild-type cytochrome c peroxidase, pH 6.0, 25°C
4.9
guaiacol
mutant N184R/W191F, pH 6.0, 25°C
5.4
guaiacol
mutant Y36A, pH 6.0, 25°C
14
guaiacol
mutant W191, pH 6.0, 25°C
1.7
H2O2
-
mutant F81W, pH 6.0, 23°C
4.3
H2O2
-
wild-type, pH 6.0, 23°C
5.5
H2O2
mutant F102W, pH 6.0, 23°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
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
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metabolism
-
bacterial diheme c-type cytochrome peroxidases catalyze the periplasmic reduction of hydrogen peroxide to water. CcpA does not seem to be part of a CymAMtrA-FccA-based electron transfer network in the periplasm of Shewanella oneidensis
evolution
MacA belongs to the family of diheme cytochrome c peroxidases
evolution
-
MacA belongs to the family of diheme cytochrome c peroxidases
-
malfunction
an enzyme knockout mutant DELTAZmcytC exhibits filamentous shapes and reduction in growth under a shaking condition at a high temperature compared to the parental strain and became hypersensitive to exogenous H2O2. Under the same condition, the mutation causes increased expression of genes for three other antioxidant enzymes. Peroxidase activity almost abolished in mutant DELTA ZmcytC. The enzyme knockout mutant strain shows activity with ubiquinol-1 as a substrate but not with reduced horse heart cytochrome c, and it shows antimycin A-sensitive NADH oxidase activity
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
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
-
physiological function
bacterial di-heme cytochrome c peroxidases (CcpAs) protect the cell from reactive oxygen species by reducing hydrogen peroxide to water
physiological function
electron transfer
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
involvement of ZmCytC in the aerobic respiratory chain via the cytochrome bc1 complex in addition to the previously proposed direct interaction with ubiquinol and its contribution to protection against oxidative stress
physiological function
-
the parasite's peroxidase LmP helps to protect the parasite from oxidative stress. LmP is a heme peroxidase that catalyzes the peroxidation of mitochondrial cytochrome c
physiological function
-
CCP1 does not affect cell respiration under cyanide treatment, but predominantly detoxifies H2O2 by glutathione. CCP1 deficiency stimulates superoxide dismutase and alcohol dehydrogenase Adh1 activity and enhances catalase-peroxidase KatG, erythroascorbate peroxidase EAPX1, and glutathione reductase GLR1 transcription by decreasing glutathione and D-erythroascorbic acid and increasing pyruvate. The CCP1-deficient mutant maintains steady-state levels of methylglyoxal. CCP1/EAPX1 double disruptants show severe growth defects due to the D-erythroascorbic acid and glutathione depletion because of pyruvate overaccumulation. CCP1-deficient and CCP1/EAPX1 double-knockout mutants show more hyphal growth than the wild-type
physiological function
-
disruption of the cytochrome c peroxidase gene causes a decrease of the membrane NADH peroxidase activity, impairs the resistance of growing culture to exogenous hydrogen peroxide and hampers aerobic growth. The mutation does not affect the activity or oxygen affinity of the respiratory chain, or the kinetics of cytochrome d reduction. Cytochrome c peroxidase does not terminate the cytochrome bc1 branch of Zymomonas mobilis
physiological function
-
increased copy number of CCP1 on chromosome XI activates respiratory metabolism and decreases pyruvate levels in an aneuploid sake yeast
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
-
physiological function
-
disruption of the cytochrome c peroxidase gene causes a decrease of the membrane NADH peroxidase activity, impairs the resistance of growing culture to exogenous hydrogen peroxide and hampers aerobic growth. The mutation does not affect the activity or oxygen affinity of the respiratory chain, or the kinetics of cytochrome d reduction. Cytochrome c peroxidase does not terminate the cytochrome bc1 branch of Zymomonas mobilis
-
additional information
-
CcP requires reductive activation for full activity. The rates of catalysis and activation differ between maltose-binding-protein-fusion and tag-free CcP and also depend on the identity of the electron donor
additional information
-
cytochrome c peroxidase-cytochrome c complex: the binding interface between LmP and LmCytc has one strong and one weak ionic interaction, the Lm redox pair is more dependent on ionic interactions than on nonpolar interactions
additional information
-
enzyme-cytochrome c protein-protein docking and modeling, overview
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
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
-
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
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purified recombinant Strep-tagged mutant enzyme H93G, and wild-type enzyme in reduced, oxidized, and semireduced states, sitting drop vapor diffusion method, 0.001 ml of 7.5 mg/ml protein is mixed with 0.001 ml of reservoir solution containing for the oxidized enzyme 0.1 M ammonium acetate buffer, pH 5.5, 1.3 M Na/K phosphate and 6% v/v of ethanol, for the ascorbate reduced enzyme 0.1 M HEPES/NaOH buffer, pH 7.5, 0.2 M ammonium acetate, and 25% w/v PEG 3350, and for the dithionite reduced enzyme 0.1 M sodium citrate buffer, pH 5.6, and 1 M ammonium phosphate, mutant MacA_H93G crystals are obtained in 1 M ammonium sulfate, pH 5.4, X-ray diffraction structure determination and analysis at 1.2-2.3 A resolution
sitting-drop vapor diffusion, 16% PEG 10000, 0.1 HEPES/NaOH, pH 7.4, 293K, wild-type enzyme, space group P1, 2.00 A resolution, mutant enzyme G94K/K97Q/R100I, space group P4321, 3.21 A resolution, mutant enzyme S134P/V135K, space group P21, 2.40 A resolution, mutant enzame S134P, space group P21, 2.40 A resolution
enzyme in complex with wild-type cytochrome c or cytochrome c mutant DELTA10LmCytc, hanging-drop vapour diffusion method, protein in 40 mM potassium phosphate, pH 6.5, 32-33% pentaerythritol ethoxylate and 4% acetone as precipitant, X-ray diffraction structure determination and analysis at 1.84-2.29 A resolution
-
the enzyme crystallizes in two different forms obtained at pH 4 and pH 5.3, corresponding to form IN, inactive, and OUT, active. In the form OUT, the calcium binding site is fully occupied by Ca2+, coordinated by seven ligands in a distorted pentagonal bipyramidal geometry, and four water molecules
Marinobacter nauticus
-
hanging-drop vapour-diffusion method
-
structures of the inactive oxidized and active mixed valence enzyme, model of the activation process
-
of mutant D37E/V45E/H181E in a metal-free form and with Co2+ at the designed Mn2+ site, mutant is a close structural model of the Mn2+ binding site in manganese peroxidase
-
diffraction limit 2.5 A
-
with 24% PEG 600, 0.2 M imidazole malate pH 5.5, 20 mM dithiothreitol
under cryogenic conditions using synchrotron radiation
-
fully oxidized form, reveals that a segment of 10 amino acids near the peroxide binding site is disordered in all four molecules of the asymmetric unit of the crystal. Flexibility in this part of the molecular scaffold correlates with the levels of activity seen in cytochrome c peroxidases characterized so far
-
hanging-drop vapour-diffusion method
-
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
-
microdialysis, in 500 mM potassium phosphate, pH 6.0, against 50 mM potassium phosphate, pH 6.0, containing 30% 2-methyl-2,4-pentanediol
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 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
structure of fluoride-inhibited enzyme
-
structure of NO-inhibited enzyme
-
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
purified recombinnat His-tagged CcpA, sitting drop vapor diffusion, mixing of 0.001 ml 7.5 mg/ml dithionite-reduced protein solution with 0.001 ml of reservoir solution containing 26% w/v PEG 2000 monomethyl ether and 0.1 M bis-(2-hydroxyethyl)-amino-tris-(hydroxymethyl)methane, pH 5.0, equilibration against 0.2 ml of reserrvoir solution, 10% v/v (2R,3R)-butanediol as a cryoprotectant, X-ray diffraction structure determination and analysis
-
modified enzyme
-
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W191F
-
less efficient at catalytic turnover than the wild-type enzyme
W191G
-
the mutant exhibits a loop-gated artificial protein cavity
W51F
-
exhibits extensive dimerization
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
H93G
site-directed mutagenesis
M297H
site-directed mutagenesis
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
H93G
-
site-directed mutagenesis
-
M297H
-
site-directed mutagenesis
-
F81W
-
modest changes in in vitro peroxidase assays
H59G
-
the distal His of the L-heme is removed
D37E/P44D/V45D
-
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
-
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
-
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
-
redesign of a manganese-binding site, ratio kcat/KM values for manganese oxidation is 0.6 per mM and s at pH 5.0
E117H
-
no enzymatic activity
E117K
-
no enzymatic activity
E117L
-
no enzymatic activity
H74M
-
no enzymatic activity, reduced redox potential. The introduced methionine does not ligate the N-terminal heme
M118H
-
no enzymatic activity
M118L
-
7.3% of wild-type activity
M278H
-
no enzymatic activity, reduced redox potential. Mutant contains two low-potential hemes
Q107L
-
no enzymatic activity
W97A
-
no enzymatic activity. W97 is the mediator of intramolecular electron transfer of the enzyme
W97F
-
no enzymatic activity. W97 is the mediator of intramolecular electron transfer of the enzyme
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
D18K
-
positive-to-negative charge-reversal mutant
D210K
-
positive-to-negative charge-reversal mutant
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
D33K
-
positive-to-negative charge-reversal mutant
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
E17K
-
positive-to-negative charge-reversal mutant
E201K
-
positive-to-negative charge-reversal mutant
E209K
-
positive-to-negative charge-reversal mutant
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
E290N
-
surface mutant, shift in reduction potential to -177 mV. Analysis of spectroscopic properties
E291K
-
positive-to-negative charge-reversal mutant
E291Q
-
surface mutant, shift in reduction potential to -162 mV. Analysis of spectroscopic properties
E32K
-
positive-to-negative charge-reversal mutant
E32Q
-
surface mutant, shift in reduction potential to -168 mV. Analysis of spectroscopic properties
E35K
-
positive-to-negative charge-reversal mutant
E98K
-
positive-to-negative charge-reversal mutant
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 |
-
site-directed mutagenesis, a distal pocket mutant
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
H52Q |
-
site-directed mutagenesis, a distal pocket mutant
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
K149D
-
positive-to-negative charge-reversal mutant
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
N184R
the N184R variant introduces potential hydrogen bonding interactions for ascorbate binding
N184R/W191F
site-directed mutagenesis
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
R31E
-
positive-to-negative charge-reversal mutant
R48E
-
distal pocket mutant, shift in reduction potential to -179 mV. Analysis of spectroscopic properties
R48L/W51L/H52L |
-
site-directed mutagenesis, a distal pocket mutant
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
W191G
provides a specific site near heme from which substrates might be oxidized
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
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
-
catalytically inactive mature Ccp1 mutant, Ccp1W191F is a more persistent H2O2 signaling protein than wild-type Ccp1
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H52L |
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site-directed mutagenesis, a distal pocket mutant
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H52Q |
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site-directed mutagenesis, a distal pocket mutant
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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
H80G
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the distal His of the L-heme is removed
H81G
mutant is highly active
M219Q/F247N
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site-directed mutagenesis
P75T/H81K/E84Q
-
site-directed mutagenesis
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
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
-
4% activity compared to the wild type enzyme, contains a high-spin, presumably five-coordinate, peroxidatic heme site
W94A
-
less than 1% of wild-type activity. Six-coordinate heme structure similar to wild-type
W94A
-
less than 1% activity compared to the wild type enzyme, the mutant retains the normal six-coordinate heme structures
D235N
-
predominantly hexacoordinate between pH 4 and pH8
D235N
-
proximal pocket mutant, shift in reduction potential to -79 mV. Analysis of spectroscopic properties
D37K
-
positive-to-negative charge-reversal mutant
D37K
-
the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c
E118K
-
positive-to-negative charge-reversal mutant
E118K
-
the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c
E290K
-
positive-to-negative charge-reversal mutant
E290K
-
the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c
H52L
-
reacts with H2O2 at a lower rate
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
-
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
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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
-
hexacoordinate, high-spin, unreactive against H2O2
R48K
-
distal pocket mutant, reduction potential -186 mV, comparable to wild-type. Analysis of spectroscopic properties
R48L
-
reacts with H2O2 at a lower rate
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
site-directed mutagenesis
W191F
-
reacts with H2O2 at a slightly higher rate
W191F
-
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
-
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
-
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
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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
-
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
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
-
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
-
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
-
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
-
an unactivated mutant devoid of the protein loop shows 10% of turnover activity of the wild type enzyme in the activated form
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
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
-
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
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
-
additional information
-
construction of a DELTAccpA mutant Shewanella oneidensis line
additional information
construction of disruption knockout mutant DELTAZmcytC, phenotype, overview
additional information
-
construction of disruption knockout mutant DELTAZmcytC, phenotype, overview
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