Information on EC 1.11.1.5 - cytochrome-c peroxidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.11.1.5
-
RECOMMENDED NAME
GeneOntology No.
cytochrome-c peroxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ferrocytochrome-c:hydrogen-peroxide oxidoreductase
A hemoprotein.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-53-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 81-176
-
-
Manually annotated by BRENDA team
strain 81-176
-
-
Manually annotated by BRENDA team
strain H99
SwissProt
Manually annotated by BRENDA team
strain H99
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene macA, i.e. gsu0466
UniProt
Manually annotated by BRENDA team
strain 617; strain 617, microaerophilically grown
-
-
Manually annotated by BRENDA team
strain Pb01 (ATCC-MYA-826)
-
-
Manually annotated by BRENDA team
strain Pb01 (ATCC-MYA-826)
-
-
Manually annotated by BRENDA team
strain LMD 52.44
-
-
Manually annotated by BRENDA team
white rot fungus
-
-
Manually annotated by BRENDA team
strain 9721
-
-
Manually annotated by BRENDA team
strain B10
-
-
Manually annotated by BRENDA team
aerobically grown
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae Red Star
-
-
-
Manually annotated by BRENDA team
synthetic construct
-
-
-
Manually annotated by BRENDA team
gene ZmcytC
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-methoxynaphthalene + H2O2
Russig's blue + 2 H2O
show the reaction diagram
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
show the reaction diagram
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
show the reaction diagram
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
?
show the reaction diagram
-
-
-
?
2,2'-azino-bis(3-ethylenbenzthiazoline-6-sulfonic acid) + H2O2
?
show the reaction diagram
2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) + H2O2
?
show the reaction diagram
-
-
-
-
?
2-aminothiazole + H2O2
?
show the reaction diagram
modified enzyme
-
-
?
ascorbate + H2O2
dehydroascorbate + H2O
show the reaction diagram
azurin + H2O2
oxidized azurin + ?
show the reaction diagram
cytochrome c + H2O2
?
show the reaction diagram
ferrocyanide + H2O2
ferricyanide + OH-
show the reaction diagram
ferrocytochrome c + CN-
?
show the reaction diagram
-
dominant binding pathway for H52L mutant, biphasic reaction
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + 2 H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
ferrocytochrome c + HCN
?
show the reaction diagram
-
dominant binding pathway for wild-type enzyme
-
-
?
ferrocytochrome c + menadione
ferricytochrome + oxidized menadione
show the reaction diagram
-
menadione can be substituted by 1,4-naphthoquinone
-
-
?
ferrocytochrome c2 + H2O2
ferricytochrome c2 + OH-
show the reaction diagram
-
-
-
-
?
ferrocytochrome c4 + H2O2
ferricytochrome c4 + OH-
show the reaction diagram
-
-
-
?
ferrocytochrome c551 + H2O2
ferricytochrome c551 + OH-
show the reaction diagram
ferrocytochrome c552 + H2O2
ferricytochrome c552 + OH-
show the reaction diagram
ferrocytochrome c553 + H2O2
ferriytochrome c553 + OH-
show the reaction diagram
-
-
-
-
?
ferrocytochrome c555 + H2O2
ferricytochrome c555 + OH-
show the reaction diagram
-
-
-
-
?
ferrocytochrome c555 + H2O2
ferriytochrome c555 + OH-
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
show the reaction diagram
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
show the reaction diagram
hydroquinone + H2O2
benzoquinone + H2O
show the reaction diagram
iso-1 ferrocytochrome c + H2O2
?
show the reaction diagram
iso-1 ferrocytochrome c mutant C102T + H2O2
iso-1 ferricytochrome c mutant C102T + 2 H2O
show the reaction diagram
-
-
-
-
?
iso-1-cytochrome c + ?
?
show the reaction diagram
-
-
-
-
?
isoniazid + H2O2
?
show the reaction diagram
-
-
-
-
?
NADH + H2O2
NAD+ + H2O
show the reaction diagram
-
-
-
?
NADPH + H2O2
NADP+ + H2O
show the reaction diagram
-
-
-
-
?
pyrogallol + H2O2
?
show the reaction diagram
reduced cytochrome c2 + H2O2
oxidized cytochrome c2 + H2O
show the reaction diagram
reduced cytochrome c551 + H2O2
oxidized cytochrome c551 + H2O
show the reaction diagram
-
-
-
-
?
reduced horse cytochrome c + H2O2
oxidized horse cytochrome c + H2O
show the reaction diagram
reduced pseudoazurin + H2O2
oxidized pseudoazurin + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
show the reaction diagram
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
show the reaction diagram
Q749D0
-
-
-
?
cytochrome c + H2O2
?
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Na+
-
maximum turnover occurs at 50 mM NaCl
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-heptyl-4-hydroxyquinoline N-oxide
-
-
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
Ag+
-
inhibition of NADH oxidizing activity
Ca2+
-
1 mM of the cation in the assay solution inhibits the oxidation of horse cytochrome c but not Pseudomonas stutzeri cytochrome c551
Cu2+
-
inhibition of NADH oxidizing activity
cyanide
cytochrome c551
-
above 0.05 mM, substrate inhibition
-
Hg2+
-
inhibition of NADH oxidizing activity
nitric oxide
-
complete suppression of activity. Nitrosyl complexes of cytochrome c produced during inhibition are sensitive to laser irradiation and are photolyzed during irradiation. Decomposition leads to partial restoration of enzyme activity
nitrite
-
2 mM, in the presence of 0.88 M of H2O2, inhibits 50% enzyme activity
Pb2+
-
inhibition of NADH oxidizing activity
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cardiolipin
FNR protein
-
expression of cytochrome c peroxidase is dependent on the combination of FNR protein and OxyR protein under conditions of oxygen starvation
-
H2O2
-
high-dose treatments with 50 mM H2O2 lead to an early increase in total CCP enzymatic activity, indicative of post-transcriptional regulation
OxyR protein
-
expression of cytochrome c peroxidase is dependent on the combination of FNR protein and OxyR protein under conditions of oxygen starvation
-
sodium dodecylsulfate
-
strict concurrency between iron-sulfur of M80 bond breaking and enzyme activity enhancement at molar ratios of sodium dodecylsulfate/cytochrome c of 0:1 to 50:1. Cardiolipin is 20times more effective than sodium dodecylsulfate
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0113
2,2-azinobis(3-ethylbenzthiazolinesulfonic acid)
-
pH 7.5, temperature not specified in the publication
0.31 - 11
ascorbate
93 - 670
cytochrome c
0.005 - 0.025
Ferrocytochrome
0.002 - 0.13
ferrocytochrome c
0.013
ferrocytochrome c550
-
-
-
510
ferrocytochrome c555
-
-
-
10 - 57
guaiacol
0.0062 - 0.51
H2O2
0.006
horse cytochrome
-
pH 7.0
-
0.042 - 0.066
horse heart ferrocytochrome c
0.0019 - 0.1
iso-1 ferrocytochrome c
5
pyrogallol
-
-
0.06
Rhodobacter capsulatus cytochrome c2
-
pH 7.0
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00007 - 0.0025
1-methoxynaphthalene
23.1
2,2-azinobis(3-ethylbenzthiazolinesulfonic acid)
Shewanella oneidensis
-
pH 7.5, temperature not specified in the publication
0.25 - 3
ascorbate
0.06 - 1510
cytochrome c
17.2 - 2000
ferrocytochrome c
17.7
ferrocytochrome c2
Rhodobacter capsulatus
-
-
3.05
ferrocytochrome c555
Methylococcus capsulatus
-
-
-
0.9 - 14
guaiacol
15.5
H2O2
Geobacter sulfurreducens
Q749D0
pH 5.5
40
horse cytochrome c
Rhodobacter capsulatus
-
pH 7.0
-
4.2 - 850.3
horse heart cytochrome c
8
pyrogallol
Saccharomyces cerevisiae
-
-
40
Rhodobacter capsulatus cytochrome c2
Rhodobacter capsulatus
-
pH 7.0
-
15.7 - 1362
yeast cytochrome c
additional information
additional information
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00015 - 0.05
cyanide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12.9
-
supernatant, pH 7.5, 25C
26.4
2,2-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) and H2O2 as electron donor and acceptor
104.6
-
; purified enzyme, pH 7.5, 25C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 10
-
by using the maximum current in the cathodic and anodic halfscans in the course of altering the pH a shift in potential is observed, at pH 7, a single redox couple (I) is dominant, but at more acidic pH values, a second couple (II) is clearly discernible at a more positive value of potential
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 hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
noncovalent association with cell surface, exposed to cell exterior
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33560
-
MALDI-TOF
34000
-
DocA, SDS-PAGE
34100 - 35240
36000
-
SDS-PAGE
36230
-
calculated
36250
-
electrospray mass spectrometry
36270
-
MALDI-TOF mass spectrometry
36580
-
electrospray mass spectrometry
37000
-
Cjj0382, SDS-PAGE
39570
-
calculated from amino acid composition
42000
-
SDS-PAGE
44000
-
amino acid analysis
48000
-
sedimentation equilibrium analysis, 0.002 mM protein, pH 6
51000
-
sedimentation velocity experiments, in the presence of EGTA
54000
-
sedimentation equilibrium analysis, 0.01 mM protein, pH 6
57500
-
gel filtration; gel filtration chromatography
59100
-
sedimentation equilibrium analysis, 0.04 mM protein, pH 6
63000
-
gel filtration
67000
-
sedimentation velocity experiments, untreated enzyme
68700
-
sedimentation equilibrium analysis, 0.04 mM protein, in the presence of 2 mM Ca2+, pH 6
69100
-
sedimentation equilibrium analysis, 0.01 mM protein, in the presence of 2 mM Ca2+, pH 6
70000
-
gel filtration
72500
-
sedimentation equilibrium analysis, 0.002 mM protein, in the presence of 2 mM Ca2+, pH 6
73000
-
sedimentation equilibrium analysis, in the presence of 5 mM Ca2+, pH 7.5
75000
-
SDS-PAGE
75030
-
predicted from cDNA sequence for dimer
78000 - 80000
-
gel filtration
80000
-
sedimentation velocity experiments, in the presence of Ca2+
87000
-
sedimentation velocity experiments, at higher protein concentrations
90000
-
gel filtration
94000
-
sedimentation velocity ultracentrifugation, with enzyme/horse heart cytochrome c ratio of 4 to 1
108000
-
sedimentation velocity ultracentrifugation, with Paracoccus cytochrome c ratio of 4 to 1
additional information
-
mutant W191F molecular weight 34196 Da after treatment with H2O2, covalent attachment of the heme (617 Da) to the apoenzyme (33561 Da)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
-
SDS-PAGE, H2O2 oxidation induces heterodimerization between cytochrome c and both wild-type and W191F enzymes, but not with W51F mutant
homodimer
monomer
monomer or dimer
polymer
-
SDS-PAGE, W51F mutant
trimer
-
SDS-PAGE, W51F mutant
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
-
-
proteolytic modification
sequence contains a leader peptide with a putative cleavage site between A41 and H42
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
resolution 1.8 A
-
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
-
resolution 2.4 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 holoenzyme
crystal structure
-
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
-
with comercial kit
-
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 10
-
-
394613
3 - 10
-
by using the maximum current in the cathodic and anodic halfscans in the course of altering the pH a shift in potential is observed, at pH 7, a single redox couple (I) is dominant, but at more acidic pH values, a second couple (II) is clearly discernible at a more positive value of potential
702343
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
8
-
CCP is not stable above pH 8.0
711231
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
15 min, 80% loss of peroxidizing activity, 50% loss of NADH oxidizing activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
crystals stable in water-saturated atmosphere for more than 5 h at 23C
-
no dimerization after 7 years
-
unstable during degassing under vacuum except in presence of detergent
-
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
-20C, 0.1 M phosphate buffer, pH 7.0, two months
-
-20C, 0.5 M phosphate buffer, pH 6
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
four-step purification protocol
-
gel filtration and ion exchange chromatography
-
high-purity V197C/C128A mutant is obtained after an anion-exchange chromatography and gel filtration
-
inner membrane proteins solubilized in sarkosyl solution and precipitated with ethanol are purified by affinity chromatography
-
native enzyme partially by preparation of mitochondria
-
partially purified
-
precipitation, DEAE-Sepharose followed by S-100 size exclusion chromatography
-
purified to homogeneity
-
purified to homogeneity in three steps
-
recombinant His-tagged CcpA from Escherichia coli strain AS457
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant N-terminally Strep-tagged protein from Escherichia coli strain BL21(DE3) by streptactin affinity 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
-
S-Sepharose column chromatography and Superdex-75 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 (DE3) cells
-
expressed in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli
expression in Escherichia coli JM109(DE3) with pETCCP coexpressed with pEC86
-
expression in Escherichia coli; mutants expressed in Escherichia coli
-
expression of maltose-binding-protein-fusion and tag-free CcP in Escherichia coli strain JM 109, the presence of the MBP tag affects the availability of certain binding sites, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expression of V197C/C128A mutant 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
-
gene ccpA, expression of His-tagged CcpA in Escherichia coli strain AS457
-
gene macA, expression as N-terminally Strep-tagged protein in Escherichia coli strain BL21(DE3)
overexpression in Escherichia coli
-
overexpression in Escherichia coli in deuterated medium
-
overexpression of modified enzyme in Escherichia coli
-
recombinant expression of wild-type and mutant enzymes
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
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
H71G/W94A
-
4% activity compared to the wild type enzyme, contains a high-spin, presumably five-coordinate, peroxidatic heme site; 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
W94A
-
less than 1% activity compared to the wild type enzyme, the mutant retains the normal six-coordinate heme structures; less than 1% of wild-type activity. Six-coordinate heme structure similar to wild-type
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
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
R48A/W51A/H52A
R48E
-
distal pocket mutant, shift in reduction potential to -179 mV. Analysis of spectroscopic properties
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
W191G
-
provides a specific site near heme from which substrates might be oxidized
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
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
-
H52L |
Saccharomyces cerevisiae Red Star
-
site-directed mutagenesis, a distal pocket mutant
-
H52Q |
Saccharomyces cerevisiae Red Star
-
site-directed mutagenesis, a distal pocket mutant
-
R48L/W51L/H52L |
Saccharomyces cerevisiae Red Star
-
site-directed mutagenesis, a distal pocket mutant
-
M219Q/F247N
-
site-directed mutagenesis
P75T/H81K/E84Q
-
site-directed mutagenesis
W191F
synthetic construct
-
study of the role of intracomplex dynamics in controlling electron transfer, use of Zn-enzyme in 1:1 complex with cytochrome c
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complete suppression of enzyme activity by niric oxide. Nitrosyl complexes of cytochrome c produced during inhibition are sensitive to laser irradiation and are photolyzed during irradiation. Decomposition leads to partial restoration of enzyme activity. nitric oxide and laser irradiation may serve as instruments for regulating the peroxidase activity of cytochrome c and, probably, apoptosis
-
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
-
reconstitution of holoenzyme
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
cytochrome c peroxidase as a platform to develop specific peroxygenation catalysts
Show AA Sequence (1251 entries)
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