1.11.1.10: chloride peroxidase
This is an abbreviated version!
For detailed information about chloride peroxidase, go to the full flat file.
Word Map on EC 1.11.1.10
-
1.11.1.10
-
fumago
-
caldariomyces
-
horseradish
-
chlorination
-
peroxidases
-
halogen
-
halide
-
haloperoxidase
-
bromination
-
lactoperoxidase
-
inaequalis
-
ferryl
-
curvularia
-
soret
-
bromoperoxidase
-
monochlorodimedone
-
low-spin
-
p450cam
-
vanadium-dependent
-
thioanisole
-
peroxidase-catalyzed
-
thiolate-ligated
-
pyrrocinia
-
oxoferryl
-
n,n-dimethylaniline
-
peroxygenases
-
agrocybe
-
vanadium-containing
-
hypohalous
-
aegerita
-
degradation
-
synthesis
-
environmental protection
-
biotechnology
- 1.11.1.10
- fumago
-
caldariomyces
- horseradish
-
chlorination
- peroxidases
-
halogen
- halide
- haloperoxidase
-
bromination
- lactoperoxidase
- inaequalis
-
ferryl
-
curvularia
-
soret
-
bromoperoxidase
- monochlorodimedone
-
low-spin
-
p450cam
-
vanadium-dependent
- thioanisole
-
peroxidase-catalyzed
-
thiolate-ligated
- pyrrocinia
-
oxoferryl
- n,n-dimethylaniline
-
peroxygenases
-
agrocybe
-
vanadium-containing
-
hypohalous
- aegerita
- degradation
- synthesis
- environmental protection
- biotechnology
Reaction
Synonyms
CCPO, Chloride peroxidase, chloroperoxidase, chloroproxidase, CPO, CPO-I, CPO2, haeme-thiolate peroxidase, heme-containing CPO, heme-thiolate chloroperoxidase, More, peroxidase, chloride, Vanadium chloride peroxidase, vCPO
ECTree
1.11.1.10 chloride peroxidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.11.1.10 - chloride peroxidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(1R,2S)-(+)-2-benzylcyclopropylmethanol + tert-butyl hydroperoxide
(1S,2R)-(+)-2-benzyl-1-formylcyclopropane + ?
-
-
-
-
?
(1R,2S)-(+)-2-ethylcyclopropylmethanol + tert-butyl hydroperoxide
(1S,2R)-(-)-2-ethyl-1-formylcyclopropane + ?
-
-
-
-
?
(1R,2S)-(+)-2-methylcyclopropanemethanol + tert-butyl hydroperoxide
(1S,2R)-(-)-2-methyl-1-formylcyclopropane + ?
-
-
-
-
?
(1R,2S)-(+)-2-propylcyclopropylmethanol + tert-butyl hydroperoxide
(1S,2R)-(-)-1-formyl-2-propylcyclopropane + ?
-
-
-
-
?
(1R,2S)-(-)-2-acetoxymethylcyclopropylmethanol + tert-butyl hydroperoxide
(1S,2R)-2-acetoxymethyl-1-formylcyclopropane + ?
-
-
-
-
?
(1R,2S)-cyclohexa-3,5-diene-1,2-diyl diacetate + tert-butyl hydroperoxide
(1S,2S,3S,6S)-7-oxabicyclo[4.1.0]hept-4-ene-2,3-diyl diacetate + (1R,2S,5R,6S)-5,6-dihydroxycyclohex-3-ene-1,2-diyl diacetate + ?
-
-
-
-
?
(1S)-3-carene + Cl- + H2O2
(1S,3R,4R,6R)-4-chloro-3,7,7-trimethyl-bicyclo[4.1.0]heptane-3-ol + H2O
-
-
-
-
?
(2E)-hex-2-en-1-ol + tert-butyl hydroperoxide
trans-(3-propyloxiran-2-yl)methanol + H2O
-
-
-
-
?
(2Z)-hex-2-en-1-ol + tert-butyl hydroperoxide
cis-(3-propyloxiran-2-yl)methanol + H2O
-
-
-
-
?
(2Z)-pent-2-en-1-ol + tert-butyl hydroperoxide
cis-2-(3-ethyloxiran-2-yl)ethanol + (3Z)-hex-3-enal + H2O
-
-
-
-
?
(3E,5E)-hepta-3,5-dien-2-one + tert-butyl hydroperoxide
(2E,4E)-6-oxohepta-2,4-dienal + (3E)-4-(3-methyloxiran-2-yl)but-3-en-2-one + (2E)-4-oxopent-2-enal
-
-
83% (2E,4E)-6-oxohepta-2,4-dienal, 4% (3E)-4-(3-methyloxiran-2-yl)but-3-en-2-one, and 13% (2E)-4-oxopent-2-enal
-
?
(3Z,5E)-hepta-3,5-dien-2-one + tert-butyl hydroperoxide
(2E,4Z)-6-oxohepta-2,4-dienal + (2E)-4-oxopent-2-enal + (2E,4E)-6-oxohepta-2,4-dienal
-
-
78% (2E,4Z)-6-oxohepta-2,4-dienal, 15% (2E)-4-oxopent-2-enal and 7% (2E,4E)-6-oxohepta-2,4-dienal
-
?
(3Z,5Z)-hepta-3,5-dien-2-one + tert-butyl hydroperoxide
(2E,4Z)-6-oxohepta-2,4-dienal + (2E)-4-oxopent-2-enal + (3Z)-4-[(2S,3S)-3-methyloxiran-2-yl]but-3-en-2-one
-
-
27% (2E,4Z)-6-oxohepta-2,4-dienal, 38% (3E)-4-(3-methyloxiran-2-yl)but-3-en-2-one and 35% (3Z)-4-[(2S,3S)-3-methyloxiran-2-yl]but-3-en-2-one
-
?
(4Z)-hex-4-en-1-ol + tert-butyl hydroperoxide
3-(3-methyloxiran-2-yl)propan-1-ol + (4Z)-hex-4-enal + H2O
-
-
-
-
?
(5R,6S)-5,6-dimethoxycyclohexa-1,3-diene + tert-butyl hydroperoxide
(1S,4S,5S,6S)-4,5-dimethoxy-7-oxabicyclo[4.1.0]hept-2-ene + ?
-
-
-
-
?
(R)-limonene + H2O2
(1S,2S,4R)-limonene-1,2-diol + (1R,2R)-4R-limonene-1,2-diol + ?
-
when the reaction is carried out in the presence of chloride ions an enhancement in the reaction rate is observed, maintaining the regioselectivity, but not the stereoselectivity. The reaction products under these conditions are (1S,2S)-4R-limonene-1,2-diol and (1R,2R)-4R-limonene-1,2-diol. In the presence of potassium chloride the limonene oxidation also occurs by the produced hypochlorite without stereoselectivity
-
-
?
(R)-limonene + H2O2
(1S,2S,4R)-limonene-1,2-diol + H2O
-
in the absence of chloride ions, at pH 3 or pH 6, the reaction is regio and stereoselective with a diasteromeric excess of more than 99% of (1S,2S)-4R-limonene-1,2-diol
-
-
?
1,2-dihydronaphthalene + tert-butyl hydroperoxide
(1R,2R)-dihydroxytetrahydronaphthalene + ?
-
-
-
-
?
1,3-cycloheptadiene + tert-butyl hydroperoxide
(1R,3R)-cyclohept-3-ene-1,2-diol + (1R,4S)cyclohept-2-ene-1,4-diol + (1R,4R)-cyclohept-2-ene-1,4-diol + ?
-
-
-
-
?
1,3-cyclooctadiene + tert-butyl hydroperoxide
cycloocta-1,4-dien-1-yl hydroperoxide + cycloocta-2,4-dien-1-ol + ?
-
-
main product is cycloocta-1,4-dien-1-yl hydroperoxide, formation of small amounts of cycloocta-2,4-dien-1-ol
-
?
2 pyrene + 3 KCl + 3 H2O2
chloropyrene + dichloropyrene + 3 KOH + 3 H2O
-
-
-
-
?
2'-deoxyuridine + Br- + H2O2
5-bromo-2'-deoxyuridine + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + HCl
?
-
-
-
-
?
2,3,5,6-tetrachloroaniline + HCl + H2O2
pentachloroaniline + H2O
-
the main product from peroxidase oxidation is a polymeric and insoluble material
-
-
?
2,3,5,6-tetrachlorophenol + HCl + H2O2
pentachlorophenol + H2O
-
the main product from peroxidase oxidation is a polymeric and insoluble material
-
-
?
2,4,6-trichlorophenol + H2O2
2,6-dichloro-1,4-benzoquinone + H2O + HCl
-
-
-
-
?
2-chlorodimedone + chloride + H2O2
1,1-dimethyl-4,4-dichloro-3,5-cyclohexanedione + 2 H2O
model substrate monochlorodimedone
-
-
?
2-methyl-4-propylcyclopentane-1,3-dione + Cl- + H2O2
2-chloro-2-methyl-4-propylcyclopentane-1,3-dione + H2O
-
reaction without appreciable stereoselectivity
-
?
3-amino-1-propanol + tert-butyl hydroperoxide
3-aminopropanal + H2O + ?
-
83.6% conversion
-
-
?
4,6-dimethyldibenzothiophene + Cl- + H2O2
?
-
the substrate exists as a monomeric and dimeric species in aqueous acetonitrile solutions. Oxidation of dimer substrate is preferred when compared to monomer oxidation
-
-
?
5-hexen-1-ol + tert-butyl hydroperoxide
5-hexenal + ?
-
-
only a small amount is produced
-
?
7-azaindole + H2O2
7-azaoxindole + H2O
-
cross-linked enzyme aggregates
-
-
?
acenaphthene + Cl- + H2O2
dichloroacenaphthene + trichloroacenaphthene + H2O
-
-
-
?
alizarin red S + Cl- + H+ + H2O2
? + 2 H2O
98.2% efficiency, degradation to nine different products
-
-
?
anthracene + 2 KCl + 2 H2O2
9,10-dichloroanthracene + 2 KOH + 2 H2O
-
-
-
-
?
benzyl-N-(2-hydroxyethyl)-carbamate + tertbutyl hydroperoxide
Cbz-glycinal + ?
-
-
-
-
?
benzyloxycarbonyl ethanolamine + tert-butyl hydroperoxide
benzyloxycarbonyl glycinal
-
-
-
-
?
biphenylene + Cl- + H2O2
dichlorobiphenylene + trichlorobiphenylene + H2O
-
-
-
?
Boc-D-methionine-methyl ester + H2O2
Boc-D-methionine-methyl ester sulfoxide + H2O
-
-
-
-
?
Boc-L-methionine-methyl ester + H2O2
Boc-L-methionine-methyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
i.e. monochlorodimedone
-
-
?
cis-2-hexen-1-ol + tert-butyl hydroperoxide
cis-2-hexenal + ?
-
-
further production of small amounts of trans-2-hexenal, cis-3-hexenal and trans-3-hexenal
-
?
cis-3-hexen-1-ol + tert-butyl hydroperoxide
cis-3-hexenal + ?
-
-
further production of small amounts of cis-2-hexenal, trans-2-hexenal and trans-3-hexenal
-
?
cis-4-hexen-1-ol + tert-butyl hydroperoxide
cis-4-hexenal + cis-4,5-epoxyhexan-1-ol + ?
-
-
further production of small amounts of trans-4,5-epoxyhexan-1-ol and trans-4-hexenal
-
?
cis-beta-methylstyrene + chloride + H2O2
?
-
-
the enzyme produced (1S2R)- and (1R2S)-epoxides at a 96:4 product ratio
-
?
cis-cyclohexa-3,5-diene-1,2-diol + tert-butyl hydroperoxide
(1R,2S,3S,4S)-cyclohex-5-ene-1,2,3,4-tetrol + ?
-
-
+ traces of (1R,2S,3S,6S)-7-oxabicyclo[4.1.0]hept-4-ene-2,3-diol
-
?
crystal violet + Cl- + H+ + H2O2
? + 2 H2O
97.7% efficiency, degradation to three products
-
-
?
estradiol + 2 bromide + 2 H2O2
2,4-bromo beta-estradiol + 4 H2O
-
-
-
?
estradiol + 2 chloride + 2 H2O2
2,4-dichloro beta-estradiol + 4 H2O
-
-
-
?
estradiol + chloride + H2O2
2-chloro beta-estradiol + 2 H2O
-
-
-
?
estradiol + chloride + H2O2
4-chloro beta-estradiol + 2 H2O
-
-
-
?
N-acetyl-L-methionine-methyl ester + H2O2
N-acetyl-L-methionine-methyl ester (RS)-sulfoxide
-
-
-
-
?
N-Cbz-3-amino-1-propanol + H2O2
N-Cbz-3-aminopropanal + H2O
-
9.7% conversion
-
-
?
N-Cbz-3-amino-1-propanol + tert-butyl hydroperoxide
N-Cbz-3-aminopropanal + H2O + ?
-
10.9% conversion
-
-
?
N-Cbz-5-aminopentanol + H2O2
N-Cbz-5-aminopentanal + H2O
-
16.3% conversion
-
-
?
N-Cbz-5-aminopentanol + tert-butyl hydroperoxide
N-Cbz-5-aminopentanal + H2O + ?
-
16.8% conversion
-
-
?
N-Cbz-6-aminohexanol + H2O2
N-Cbz-6-aminohexanal + H2O
-
12.3% conversion
-
-
?
N-Cbz-6-aminohexanol + tert-butyl hydroperoxide
N-Cbz-6-aminohexanal + H2O + ?
-
9.4% conversion
-
-
?
N-chloroacetyl-L-methionine-methyl ester + H2O2
N-chloroacetyl-L-methionine-methyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-formyl-L-methionine-methyl ester + H2O2
N-formyl-L-methionine-methyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-D-ethionine-methyl ester + H2O2
N-methoxycarbonyl-D-ethionine-methyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-D-methionine-ethyl ester + H2O2
N-methoxycarbonyl-D-methionine-ethyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-D-methionine-methyl ester + H2O2
N-methoxycarbonyl-D-methionine-methyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-D-methionine-n-butyl ester + H2O2
N-methoxycarbonyl-D-methionine-n-butyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-D-methionine-n-propyl ester + H2O2
N-methoxycarbonyl-D-methionine-n-propyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-L-ethionine-ethyl ester + H2O2
N-methoxycarbonyl-L-ethionine-ethyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-L-ethionine-methyl ester + H2O2
N-methoxycarbonyl-L-ethionine-methyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-L-methionine-ethyl ester + H2O2
N-methoxycarbonyl-L-methionine-ethyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-L-methionine-methyl ester + H2O2
N-methoxycarbonyl-L-methionine-methyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-L-methionine-n-butyl ester + H2O2
N-methoxycarbonyl-L-methionine-n-butyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-L-methionine-n-pentyl ester + H2O2
N-methoxycarbonyl-L-methionine-n-pentyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-L-methionine-n-propyl ester + H2O2
N-methoxycarbonyl-L-methionine-n-propyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
pentachlorophenol + HCl + H2O
?
-
the main product from peroxidase oxidation is a polymeric and insoluble material
-
-
?
RH + chloride + H2O2
RCl + 2 H2O
-
-
-
?
styrene + H2O2
?
-
native enzyme is conjugated with polystyrene to form a surfactant-like structure that self assembled at oil-water interfaces. The interface-assembly of the enzyme improves the overall catalytic efficiency as compared to traditional biphasic reactions with enzymes contained in bulk aqueous phase. The interfacial placement of the enzyme can suppress unwanted side reactions including the hydrolysis of the styrene epoxide product
-
-
?
sulfur mustard + chloride + H2O2
sulfur mustard sulfoxide + H2O
-
-
-
-
?
thioanisole + HCl + H2O2
?
-
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
-
-
?
thymine + Br- + H2O2
5-bromo-6-hydroxy-5,6-dihydrothymine + H2O
-
-
-
?
thymol + Br- + H2O2
3-bromothymol + 4-bromothymol + 6-bromothymol + H2O
-
-
-
?
trans-2-hexen-1-ol + tert-butyl hydroperoxide
trans-2-hexenal + ?
-
-
further production of small amounts of cis-2-hexenal,cis-3-hexenal and trans-3-hexenal
-
?
trans-2-phenylcyclopropylmethanol + tert-butyl hydroperoxide
?
-
formation of the aldehyde with poor enantioselectivity
-
-
?
trans-3,4-dimethoxycinnamic acid + Br- + H2O2 + H+
DL-1,1-dibromo-2-hydroxy-2-(3,4-dimethoxy-5-bromophenyl)ethane + DL-1,1-dibromo-2-hydroxy-2-(3,4-dimethoxyphenyl)ethane + 2-bromo-3-hydroxy-3-(3,4-dimethoxyphenyl)propionic acid + H2O
-
-
-
?
trans-3,4-dimethoxycinnamic acid + Cl- + H2O2 + H+
trans-1-chloro-2-(3,4-dimethoxy-5-chlorophenyl)ethylene + trans-1-chloro-2-(3,4-dimethoxyphenyl)ethylene + DL-1,1-dichloro-2-hydroxy-2-(3,4-dimethoxyphenyl)ethane
-
-
-
?
trans-3-hexen-1-ol + tert-butyl hydroperoxide
trans-3-hexenal + ?
-
-
further production of small amounts of cis-3-hexenal, trans-2-hexenal and cis-3-hexenal
-
?
trans-4-hexen-1-ol + tert-butyl hydroperoxide
trans-2-(3-ethyloxiran-2-yl)ethanol + (3E)-hex-3-enal + H2O
-
-
-
-
?
trans-4-hexen-1-ol + tert-butyl hydroperoxide
trans-4,5-epoxyhexan-1-ol + trans-4-hexenal + H2O + ?
-
-
-
-
?
trans-4-hexen-1-ol + tert-butyl hydroperoxide
trans-4-hexenal + trans-4,5-epoxyhexan-1-ol + ?
-
-
further production of small amounts of cis-4,5-epoxyhexan-1-ol and cis-4-hexenal
-
?
trans-4-hydroxycinnamic acid + Br- + H+ + H2O2
trans-1-bromo-2-(4-hydroxyphenyl)ethylene + H2O
-
-
-
?
trans-4-hydroxycinnamic acid + Cl- + H+ + H2O2
trans-1-chloro-2-(4-hydroxyphenyl)ethylene + H2O
-
-
-
?
trans-4-methoxy-cinnamic acid + Br- + H+ + H2O2
2,3-dihydroxy-3-(4-methoxyphenyl)propionic acid + DL-1,1-dibromo-2-hydroxy-2-(4-methoxyphenyl)ethane + H2O
-
-
-
?
trans-cinnamic acid + H2O2 + Br- + H+
trans-1-bromo-2-phenylethylene + erythro-2-bromo-3-hydroxy-3-phenylpropionic acid + H2O
-
-
-
?
tyrosine + Cl- + H2O2
monochlorotyrosine + dichlorotyrosine
-
-
-
?
[2-(2-bromoethyl)cyclopropyl]methanol + tert-butyl hydroperoxide
2-(2-bromoethyl)cyclopropanecarbaldehyde + ?
-
-
-
-
?
[2-(3-bromopropyl)cyclopropyl]methanol + tert-butyl hydroperoxide
2-(3-bromopropyl)cyclopropanecarbaldehyde + ?
-
-
-
-
?
[2-(hydroxymethyl)cyclopropyl]methyl acetate + tert-butyl hydroperoxide
(2-formylcyclopropyl)methyl acetate + ?
-
-
-
-
?
[3.2.0]hept-2-en-6-one + Br- + H2O2
(1S,2S,3S,5S)-3-bromo-2-hydroxybicyclo[3.2.0]heptan-6-one + H2O
-
-
-
?
benzyl N-(2-hydroxyethyl)carbamate + H2O2
? + H2O
-
24.4% conversion
-
-
?
benzyl N-(2-hydroxyethyl)carbamate + H2O2
? + H2O
-
25.7% conversion
-
-
?
benzyl N-(2-hydroxyethyl)carbamate + tert-butyl hydroperoxide
? + H2O
-
18.8% conversion
-
-
?
benzyl N-(2-hydroxyethyl)carbamate + tert-butyl hydroperoxide
? + H2O
-
77.9% conversion
-
-
?
gentian violet + Cl- + H+ + H2O2
? + 2 H2O
-
96.5% efficiency
-
-
?
indole + H2O2
2-oxoindole + H2O
-
chloroperoxidase at neutral and at acidic pH is able to catalytically scavenge peroxynitrite, although the reaction cycle is not fully clarified
-
-
?
isoplagiochin C + Cl- + H2O2
?
-
incorporation of 1-6 chlorine atoms
-
-
?
isoplagiochin C + Cl- + H2O2
?
-
incorporation of 1-6 chlorine atoms
-
-
?
methyl orange + Cl- + H+ + H2O2
? + 2 H2O
-
98.1% efficiency
-
-
?
monochlorodimedon + chloride + H2O2
dichlorodimedon + 2 H2O
-
-
-
?
monochlorodimedon + chloride + H2O2
dichlorodimedon + 2 H2O
H2O2 activation of the heme group
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
-
-
-
?
monochlorodimedone + Br- + H2O2
monobromo-monochlorodimedone + H2O
-
-
-
-
?
monochlorodimedone + Br- + H2O2
monobromo-monochlorodimedone + H2O
-
-
-
-
?
monochlorodimedone + chloride + H2O2
dichlorodimedone + H2O
-
-
-
-
?
monochlorodimedone + chloride + H2O2
dichlorodimedone + H2O
-
-
-
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?
monochlorodimedone + Cl- + H2O2
dichlorodimedone + H2O
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nuclear fast red + Cl- + H+ + H2O2
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96.7% efficiency
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in the absence of organic substrates, chloroperoxidase catalyzes the peroxidation of chloride and bromide ion to molecular chlorine and bromine. However these molecular species are not formed as intermediates in the enzymic halogenation of organic halogen-acceptor substrates
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oxidation of phenolics and related compounds with H2O2
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oxidation of substituted indoles and sulfides with H2O2
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peroxidation of para-substituted phenolic compounds
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evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
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the enzyme also catalyzes peroxidase and catalase reaction in the absence of halide substrates
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catalyzes the oxidation iodide to iodine
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the enzyme also catalyzes the dismutation of chlorine dioxide into chloride, chlorate and oxygen
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transformation of aromatic pollutants into chlorinated derivatives by microbial enzymes may occur in polluted sites. This biocatalytic process should be considered because the toxicity and environmental impact of aromatic compounds may be increased
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in halide-independent oxidation reactions, CPO uses H2O2 or other organic peroxides as the source of oxygen without requiring cofactors
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no reaction with N-acetyl-L-methionine, N-methoxycarbonyl-L-methionine, N-phthaloyl-L-methionine
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a mechanistic comparison between cytochrome P450- and chloroperoxidase-catalyzed N-dealkylation of N,N-dialkyl anilines
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catalyzes the unspecific chlorination, bromination, and iodation (but no fluorination) of a variety of electrophilic organic substrates via hypohalous acid as actual halogenating agent. In the absence of halide, CPO resembles cytochrome P450s and epoxidizes and hydroxylates activated substrates such as organic sulfides and olefins. Aromatic rings are not susceptible to CPO-catalyzed oxygen-transfer
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crystal structure of the reaction intermediate compound 0 determined at a resolution of 1.75 A
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in the presence of enzyme and H2O2, but in the absence of chloride or bromide, the terpene alcohols geraniol, nerol and citronellol are substrates of CPO and are oxidized to the corresponding aldehydes geranial, neral and citronellal, respectively
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the enzyme can dehalogenate trihalophenols and p-halophenols. CCPO catalyzes H2O2-dependent defluorination, debromination, and deiodination reactions. Two main products, p-benzoquinone (minor) and the halophenol dimer (major), are observed for all p-halophenol-CCPO-catalyzed dehalogenation reactions
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exhibits catalase, peroxidase and cytochrome P450 activities besides the halogenation reaction
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oxidation of hydrophobic substrates in alpha-pinene-based ternary systems using tert-butyl hydroperoxide (compound/main product: cis-2-heptene/cis-2-heptene oxide, 1-methyl-cyclohexene/1-methyl-1,2-dihydroxycyclohexane, geraniol/geranial, nerol/neral, perillyl alcohol/perillyl aldehyde)
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oxidative dehalogenation of trihalophenols and p-halophenols
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CPO is a peroxide-dependent chlorinating enzyme and it also catalyzes peroxidase-, catalase-, and cytochrome P450-type reactions of dehydrogenation, hydrogen peroxide decomposition, and oxygen insertion, respectively
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the enzyme is incapable of catalyzing the halogenation of indole
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formation and protonation of compound X, a hypochlorite heme adduct intermediate existing during CPO-catalyzed halide-dependent reactions, significantly lowers the reaction barrier and increases the efficiency of CPO-catalyzed orange G degradation
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production of polyhalogenated carbazoles (PHCs) from halogenation of carbazole in the presence of bromide and/or chloride under the catalysis of chloroperoxidase (CPO) isolated from the marine fungus Caldariomyces fumago, see also EC 1.11.1.18. A total of 25 congeners including mono-to tetra-substituted chlorinated, brominated, and mixed halogenated carbazoles (with substitution patterns of -BrCl, -BrCl2, -BrCl3, -Br2Cl, -Br2Cl2, and -Br3Cl) are produced from the reactions under various conditions. The PHC product profiles are apparently dependent on the halide concentrations. In the CPO-mediated chlorination of carbazole, 3-mono- and 3,6-dichlorocarbazoles predominated in the formation products. In addition to the less abundant mixed halogenated carbazoles (-Br2Cl), 1,3,6-tri- and 1,3,6,8-tetrabromocarbazoles are the dominant products in reactions containing both Br- and Cl-
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the immobilized enzyme CPO catalyzes degradation of mesotrione (2-[(4-methylsulfonyl)-2-nitrobenzoyl]cyclohexan-1,3-dione) in wastewater
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asymmetric sulfoxidation of 2-(diphenylmethylthio) acetamide to (R)-modafinil
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chloroperoxidase from Caldariomyces fumago catalyzes the selective oxidation of furfuryl alcohols in an Achmatowicz-type ring expansion. In combination with glucose oxidase as oxygen-activating biocatalyst, a purely enzymatic, aerobic protocol for the synthesis of 6-hydroxypyranone building blocks is obtained. Thanks to an only modest stereochemical bias of the oxygenating heme protein, optically active alcohols of either configuration are converted without a significant mismatch opening up opportunities for enantioselective multienzymatic cascades. Balancing the oxidase-driven aerobic activation, extended enzyme half-lives and productive conversion of poorly soluble and slowly reacting substrates can be achieved with high yields of the six-membered O-heterocycles. The chloroperoxidase from Caldariomyces fumago (CPO) acts as peroxidase-P450 functional hybrid. Enantiodiscrimination in the oxidative conversion of racemic furfuryl alcohols by enzyme CPO in a coupled assay with the glucose oxidase (GOx) from Aspergillus niger, substrate specificity, overview
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CPO is a haeme-thiolate peroxidase requiring the presence of H2O2 to form an activated enzymatic species, responsible for oxidising either halides or organic substrates. CPO catalyses the halogenation of estrogens at comparable rates to other aromatic compounds
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CPO-catalyzed degradation of the dyes Orange G, acid blue 45, or crystal violet from wastewater samples, kinetics at pH 3.0, 20°C
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LC-MS/MS and gas chromatography-mass spectrometry (GC-MS) are used for product identification, overview. Hydroxylated polybrominated diphenyl ethers (diOH-PBDEs) and hydroxylated polybrominated biphenyls (diOH-PBBs) formed by dihydroxyl group substitutions in the ortho-positions relative to the diphenyl ether bond or the single bond in biphenyl, may undergo intramolecular cyclization
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theoretical analysis of the influence of the proximal pockets of cytochrome P450CAM and chloroperoxidase (CPO) on the relative favorability of catalytic epoxidation and allylic hydroxylation of olefins, a type of alkene oxidation selectivity. Quantum mechanical models of the active site are employed to isolate the proximal pocket's influence on the barrier for the selectivity-determining step for each reaction, using cyclohexene and cis-beta-methylstyrene as substrates. The proximal pocket shows preference for epoxidation, the largest value being for CPO, converting the active heme-thiolate moiety from being intrinsically hydroxylation-selective to being intrinsically epoxidation-selective. The proximal pocket is the key determinant of alkene oxidation selectivity. The selectivity for epoxidation can be rationalized in terms of the proximal pocket's modulation of the thiolate's electron push and consequent influence on the heme redox potential and the basicity of the trans ligand. The ratio of epoxidation to allylic hydroxylation products [C=C/C-H ratio or alkene oxidation selectivity (AOS)] is measured for several substrates, including propene, 2-butene, cyclohexene, and cis-beta-methylstyrene (CBMS), for catalysis by CPO or P450 isozymes, e.g. oxidation reactions of cyclohexene with compound I. The AOS varies according to substrate and enzyme, on average, epoxidation is slightly favored. The substrates studied lack strongly orienting interactions with residues of the distal binding pocket, consequently, the intrinsic reactivity of the heme-thiolate group with these substrates may make a significant contribution, perhaps the dominant one, to the AOS of P450 and CPO toward them
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formation and protonation of compound X, a hypochlorite heme adduct intermediate existing during CPO-catalyzed halide-dependent reactions, significantly lowers the reaction barrier and increases the efficiency of CPO-catalyzed orange G degradation
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epoxidations of indene, styrene, 2-chlorostyrene, 3-chlorostyrene, 4-chlorostyrene, 4-bromostyrene, and naphthalene using Musa paradisiaca plant juice chloroperoxidase in the presence of H2O2 and t-butyl peroxide as oxidants. The yield of styrene oxide in the presence of H2O2 is 44%. The relative affinities of the enzyme for these substrates are in the following order: styrene < 4-chlorostyrene < 3-chlorostyrene < 2-chlorostyrene. Epoxidation by heme chloroperoxidase is the most convenient and promising enzymatic process
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