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Information on EC 1.13.11.49 - chlorite O2-lyase
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1.13.11.49 chlorite O2-lyaseIUBMB Comments
Reaction occurs in the reverse direction in chlorate- and perchlorate-reducing bacteria. There is no activity when chlorite is replaced by hydrogen peroxide, perchlorate, chlorate or nitrite. The term 'chlorite dismutase' is misleading as the reaction does not involve dismutation/disproportionation. Contains iron and protoheme IX.
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Word Map
- 1.13.11.49
- perchlorate
- chlorate
- dechloromonas
-
perchlorate-reducing
- dismutases
- clo2
-
dismutation
-
high-spin
-
low-spin
- dechloratans
- defluvii
-
chlorate-reducing
- nitrospira
- ideonella
- aromatica
- azospira
-
hemqs
- environmental protection
- molecular biology
- biotechnology
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
chlorite dismutase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
chlorite dismutase
CLD
dimutase, chlorite
-
-
-
-
HemQ
Pfam chlorite dismutase
PitA
chlorite dismutase
-
-
-
-
chlorite dismutase
-
-
chlorite dismutase
Dechlorosoma sp. KJ / ATCC BAA-592
-
-
-
chlorite dismutase
Stutzerimonas chloritidismutans AW-1 / DSM 13592
-
-
-
chlorite dismutase
Stutzerimonas chloritidismutans AW-1(T)
-
-
-
CLD
Stutzerimonas chloritidismutans AW-1 / DSM 13592
-
-
-
CLD
Stutzerimonas chloritidismutans AW-1(T)
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chloride + O2 = chlorite
reaction occurs in the reverse direction in chlorate- and perchlorate-reducing bacteria. There is no activity when chlorite is replaced by hydrogen peroxide, perchlorate, chlorate or nitrite. The term 'chlorite dismutase' is misleading as the reaction does not involve dismutation/disproportionation. Contains iron and protoheme IX
-
-
-
chloride + O2 = chlorite
reaction mechanism and active site structure, Arg173 plays a key role in (i) controlling of ligand and substrate access and binding and (ii) in chlorite dismutation reaction, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
chloride:oxygen oxidoreductase
Reaction occurs in the reverse direction in chlorate- and perchlorate-reducing bacteria. There is no activity when chlorite is replaced by hydrogen peroxide, perchlorate, chlorate or nitrite. The term 'chlorite dismutase' is misleading as the reaction does not involve dismutation/disproportionation. Contains iron and protoheme IX.
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CAS REGISTRY NUMBER
COMMENTARY
190208-21-0
-
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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
chloride + O2
chlorite
-
chlorite dismutase catalyzes O2 release from chlorite with exquisite efficiency and specificity
-
-
r
chloride + O2
chlorite
-
chlorite dismutase catalyzes O2 release from chlorite with exquisite efficiency and specificity, the protonation state of the heme environment influences dioxygen formation. The reaction proceeds via an acid-base transition with pKa of 8.7, spectroscopic properties, ligand binding affinities, and steady-state kinetics, unique structure-activity model, overview
-
-
r
chloride + O2
chlorite
chlorite dismutase is a unique heme enzyme which transforms chlorite to chloride and molecular oxygen
-
-
r
chloride + O2
chlorite
Arg173 plays a key role in (i) controlling of ligand and substrate access and binding and (ii) in chlorite dismutation reaction, mechanism, overview. The flexible residue modulates the electrostatic potential and size of the active site entrance and might be involved in keeping transiently formed hypochlorite in place for final molecular oxygen and chloride formation
-
-
r
chlorite
chloride + O2
-
-
reaction provides oxygen for aerobic benzene biodegradation
-
?
chlorite
chloride + O2
-
-
reaction provides oxygen for aerobic benzene biodegradation
-
?
chlorite
chloride + O2
catalytic mechanism via ferryl species and ClO--anion
-
-
?
chlorite
chloride + O2
the enzyme is highly specific for chlorite
-
-
?
chlorite
chloride + O2
catalytic mechanism via ferryl species and ClO--anion
-
-
?
chlorite
chloride + O2
-
-
highly specific (no 18O from 18O-labeled water), no other side products with 18O-labeled ClO2- detectable
-
?
chlorite
chloride + O2
-
the heme enzyme rapidly converts chlorite to chloride and O2, suggesting a simple approach to overcoming both the technical difficulties in the systematic variation of the O2 concentration and its modest solubility
-
-
?
chlorite
chloride + O2
Stutzerimonas chloritidismutans
-
-
degradation of n-alkane or intermediates + chlorate
-
?
chlorite
chloride + O2
Stutzerimonas chloritidismutans
-
-
water is not involved in the O2-building reaction (no inclusion of 18O-isotope from labeled water)
-
?
chlorite
chloride + O2
Stutzerimonas chloritidismutans AW-1 / DSM 13592
-
-
degradation of n-alkane or intermediates + chlorate
-
?
chlorite
chloride + O2
Stutzerimonas chloritidismutans AW-1 / DSM 13592
-
-
water is not involved in the O2-building reaction (no inclusion of 18O-isotope from labeled water)
-
?
chlorite
chloride + O2
Stutzerimonas chloritidismutans AW-1(T)
-
-
degradation of n-alkane or intermediates + chlorate
-
?
additional information
?
-
the enzyme can reversibly bind acetate to form a green colored high spin ferric complex
-
-
-
additional information
?
-
-
PitA possesses both chlorite dismutase-related (N-terminus) and antibiotic biosynthesis monooxygenase-related (C-terminus) activities
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-
?
additional information
?
-
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PitA possesses both chlorite dismutase-related (N-terminus) and antibiotic biosynthesis monooxygenase-related (C-terminus) activities
-
-
?
additional information
?
-
upon reduction of chlorite, hypochlorite is formed and kept in the reaction sphere for recombination with the oxoiron(IV) group of Compound I. Approximately one molecule of HOCl per 100 full cycles escapes and reacts with both the prosthetic group and the protein moiety, leading to irreversible inactivation of Cld is observed which is more pronounced with an increase in pH. HOCl traps like methionine can rescue the enzyme from inactivation
-
-
?
additional information
?
-
chlorite binding to ferric Cld occurs spontaneously and residue Arg173 is important for recognition and to impair hypochlorite leakage from the reaction sphere
-
-
?
additional information
?
-
-
chlorite binding to ferric Cld occurs spontaneously and residue Arg173 is important for recognition and to impair hypochlorite leakage from the reaction sphere
-
-
?
additional information
?
-
-
although its sequence is highly similar to functional chlorite dismutases, the HemQ protein has no steady state reactivity with chlorite, very modest reactivity with H2O2 or peracetic acid, and no observable transient intermediates
-
-
?
additional information
?
-
-
HemQ uses heme or porphyrin-like organic molecules as substrates. At pH 6.8, the enzyme exhibits relatively weak peroxidase activity with the reductant 2,2'-azino-bis[3-ethylbenzthiazoline-6-sulfonic acid], kinetics, overview
-
-
?
additional information
?
-
-
although its sequence is highly similar to functional chlorite dismutases, the HemQ protein has no steady state reactivity with chlorite, very modest reactivity with H2O2 or peracetic acid, and no observable transient intermediates
-
-
?
additional information
?
-
-
HemQ uses heme or porphyrin-like organic molecules as substrates. At pH 6.8, the enzyme exhibits relatively weak peroxidase activity with the reductant 2,2'-azino-bis[3-ethylbenzthiazoline-6-sulfonic acid], kinetics, overview
-
-
?
additional information
additional information
-
-
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) is a diagnostic for peroxidase reactivity, 100 mM phosphate buffer (pH 6.8) and citrate phosphate buffer (pH 4.0)
no relevant peroxidase reactivity products, only in the presence of oxidant peroxyacetic acid peroxidase reactivity products are obtained (1.6 equivalents per mol oxidant)
-
?
additional information
additional information
-
-
guaiacol is a diagnostic for peroxidase reactivity, 100 mM phosphate buffer (pH 6.8) and citrate phosphate buffer (pH 4.0)
no relevant peroxidase reactivity products, only in the presence of oxidant peroxyacetic acid peroxidase reactivity products are obtained (1.6 equivalents per mol oxidant)
-
?
additional information
additional information
-
-
monochlorodimedone is a diagnostic for halogenation reactivity, 100 mM phosphate buffer (pH 6.8) and citrate phosphate buffer (pH 4.0)
no halogenation is observed, not even when Cl-, Br-, or I- are added in excess (10 mM) under the same conditions or when oxidants such as peroxyacetic acid or H2O2 are added
-
?
additional information
additional information
-
-
peroxyacetic acid with chlorite
in excess of peroxyacetic acid the formation of two high-valent ferryl intermediates can be observed with stopped-flow UV-vis spectrophotometry in 0.1 M sodium phosphate buffer, pH 7.0, 10°C and with electron paramagnetic resonance in 20% ethylene glycol, 80% 0.010 M phosphate buffer, pH 7.14, addition of substrate and enzyme at 4°C, flash freezing in liquid N2 for analysis
-
?
additional information
additional information
-
-
thioanisole is a diagnostic for peroxygenase reactivity, 100 mM phosphate buffer (pH 6.8) and citrate phosphate buffer (pH 4.0)
no relevant sulfoxide products that would point to peroxygenase reactivity, only in the presence of oxidant peroxyacetic acid sulfoxide formation is observed (0.247 sulfoxide per mol oxidant)
-
?
additional information
additional information
-
-
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) is a diagnostic for peroxidase reactivity, 100 mM phosphate buffer (pH 6.8) and citrate phosphate buffer (pH 4.0)
no relevant peroxidase reactivity products, only in the presence of oxidant peroxyacetic acid peroxidase reactivity products are obtained (1.6 equivalents per mol oxidant)
-
?
additional information
additional information
-
-
guaiacol is a diagnostic for peroxidase reactivity, 100 mM phosphate buffer (pH 6.8) and citrate phosphate buffer (pH 4.0)
no relevant peroxidase reactivity products, only in the presence of oxidant peroxyacetic acid peroxidase reactivity products are obtained (1.6 equivalents per mol oxidant)
-
?
additional information
additional information
-
-
monochlorodimedone is a diagnostic for halogenation reactivity, 100 mM phosphate buffer (pH 6.8) and citrate phosphate buffer (pH 4.0)
no halogenation is observed, not even when Cl-, Br-, or I- are added in excess (10 mM) under the same conditions or when oxidants such as peroxyacetic acid or H2O2 are added
-
?
additional information
additional information
-
-
peroxyacetic acid with chlorite
in excess of peroxyacetic acid the formation of two high-valent ferryl intermediates can be observed with stopped-flow UV-vis spectrophotometry in 0.1 M sodium phosphate buffer, pH 7.0, 10°C and with electron paramagnetic resonance in 20% ethylene glycol, 80% 0.010 M phosphate buffer, pH 7.14, addition of substrate and enzyme at 4°C, flash freezing in liquid N2 for analysis
-
?
additional information
additional information
-
-
thioanisole is a diagnostic for peroxygenase reactivity, 100 mM phosphate buffer (pH 6.8) and citrate phosphate buffer (pH 4.0)
no relevant sulfoxide products that would point to peroxygenase reactivity, only in the presence of oxidant peroxyacetic acid sulfoxide formation is observed (0.247 sulfoxide per mol oxidant)
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chloride + O2
chlorite
-
chlorite dismutase catalyzes O2 release from chlorite with exquisite efficiency and specificity
-
-
r
chloride + O2
chlorite
chlorite dismutase is a unique heme enzyme which transforms chlorite to chloride and molecular oxygen
-
-
r
chlorite
chloride + O2
-
-
reaction provides oxygen for aerobic benzene biodegradation
-
?
chlorite
chloride + O2
-
-
reaction provides oxygen for aerobic benzene biodegradation
-
?
chlorite
chloride + O2
catalytic mechanism via ferryl species and ClO--anion
-
-
?
chlorite
chloride + O2
catalytic mechanism via ferryl species and ClO--anion
-
-
?
chlorite
chloride + O2
-
-
highly specific (no 18O from 18O-labeled water), no other side products with 18O-labeled ClO2- detectable
-
?
chlorite
chloride + O2
-
the heme enzyme rapidly converts chlorite to chloride and O2, suggesting a simple approach to overcoming both the technical difficulties in the systematic variation of the O2 concentration and its modest solubility
-
-
?
chlorite
chloride + O2
Stutzerimonas chloritidismutans
-
-
degradation of n-alkane or intermediates + chlorate
-
?
chlorite
chloride + O2
Stutzerimonas chloritidismutans
-
-
water is not involved in the O2-building reaction (no inclusion of 18O-isotope from labeled water)
-
?
chlorite
chloride + O2
Stutzerimonas chloritidismutans AW-1 / DSM 13592
-
-
degradation of n-alkane or intermediates + chlorate
-
?
chlorite
chloride + O2
Stutzerimonas chloritidismutans AW-1 / DSM 13592
-
-
water is not involved in the O2-building reaction (no inclusion of 18O-isotope from labeled water)
-
?
chlorite
chloride + O2
Stutzerimonas chloritidismutans AW-1(T)
-
-
degradation of n-alkane or intermediates + chlorate
-
?
additional information
?
-
upon reduction of chlorite, hypochlorite is formed and kept in the reaction sphere for recombination with the oxoiron(IV) group of Compound I. Approximately one molecule of HOCl per 100 full cycles escapes and reacts with both the prosthetic group and the protein moiety, leading to irreversible inactivation of Cld is observed which is more pronounced with an increase in pH. HOCl traps like methionine can rescue the enzyme from inactivation
-
-
?
additional information
?
-
-
although its sequence is highly similar to functional chlorite dismutases, the HemQ protein has no steady state reactivity with chlorite, very modest reactivity with H2O2 or peracetic acid, and no observable transient intermediates
-
-
?
additional information
?
-
-
although its sequence is highly similar to functional chlorite dismutases, the HemQ protein has no steady state reactivity with chlorite, very modest reactivity with H2O2 or peracetic acid, and no observable transient intermediates
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
HemQ's equilibrium affinity for heme is in the low micromolar range. Holo-HemQ reconstituted with heme exhibits heme lysis after less than 50 turnovers with peroxide and less than 10 turnovers with chlorite. The heme-free apoprotein aggregates or unfolds over time. HemQ uses heme or porphyrin-like organic molecules as substrates. Heme in HemQ degrades in the presence of relatively small numbers of equivalents of H2O2, chlorite, or peracetic acid
heme
-
at pH 6.0, ferric Cld exhibits a Soret band maximum at 405 nm, a broad alpha/beta band envelope at 505 nm with a small shoulder at 540 nm, and a charge transfer band at 645 nm
heme
resting ferric high-spin axially symmetric heme enzyme, standard reduction potential of the Fe(III)/Fe(II) couple of -126 mV at pH 7.0
heme
wild-type Cld shows a variety of low- and high-spin ferric heme forms. Addition of an axial ligand, such as azide or imidazole, removes this heterogeneity almost entirely
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
(NH4)2SO4
Stutzerimonas chloritidismutans
-
activity increases with increasing salt concentration up to 2 M
Fe2+
Iron
Na2SO4
Stutzerimonas chloritidismutans
-
activity increases with increasing salt concentration up to 2 M
NaClO3
Stutzerimonas chloritidismutans
-
decreasing activity with increasing salt concentration
NaNO3
Stutzerimonas chloritidismutans
-
decreasing activity with increasing salt concentration
potassium phosphate
Stutzerimonas chloritidismutans
-
activity increases with increasing salt concentration up to 1 M salt, decrease beyond 1 M salt
Sodium phosphate
Stutzerimonas chloritidismutans
-
activity increases with increasing salt concentration up to 1 M salt, decrease beyond 1 M salt
additional information
Stutzerimonas chloritidismutans
-
kosmotropic salts such as sulfate and phosphate stabilize protein structures by water-structuring effects of the ions, chaotropic salts such as nitrate and chlorate reduce the activity, no effect of NaCl, NH4Cl, and NaHCO3 (up to 1.5 M) on enzyme activity
Iron
-
spectroscopic evidence is presented for a proximal histidine coordinating the heme iron center of the enzyme. The bond between the proximal histidine and the iron is weak and can be broken upon binding of NO. The midpoint potential, Em (Fe3+/2+) = -23 mV
Iron
vibrational frequency correlations between either ny(FeIII-F) or ny(FeIII-OH) and ny(FeII-His) orthogonalize proximal and distal effects on the bonding between iron and exogenous pi-donor ligands
Iron
-
vibrational frequency correlations between either ny(FeIII-F) or ny(FeIII-OH) and ny(FeII-His) orthogonalize proximal and distal effects on the bonding between iron and exogenous pi-donor ligands
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
substrate inhibition at higher concentrations over 0.2 mM
H2O2
Stutzerimonas chloritidismutans
-
at 70 microM 6% inhibition, at 700 microM 37% inhibition
azide
Stutzerimonas chloritidismutans
-
at 70 microM 44% inhibition, at 700 microM 89% inhibition
chloride
upon cooperative binding of Cl-, Cld remains pentacoordinate and high-spin
chloride
-
cooperative binding of Cl- to Cld drives formation of a hexacoordinate, high-spin aqua heme
chloride
weak mixed inhibitor that modifies the EPR signal of as-prepared samples
Chlorite
above 0.1 mM chlorite (5000fold excess) irreversible inactivation is observed
Chlorite
-
irreversibly inactivates the enzyme after 17000 turnovers (per heme) and with a half-life of 0.39 min, resulting in bleaching of the heme chromophore. Guaiacol offers incomplete protection of the enzyme from inactivation
Chlorite
-
chlorite acts a suicide substrate. Loss of activity is correlated with destruction of the heme and also some degree of protein damage
cyanide
Stutzerimonas chloritidismutans
-
at 70 microM 83% inhibition, at 700 microM 95% inhibition
EDTA
Stutzerimonas chloritidismutans
-
at 70 microM 13% inhibition, at 700 microM 30% inhibition
fluoride
fluoride coordinates to the heme iron in Cld exhibiting ny(FeIII-F) band at 390 per cm. Strong H-bond donation happens to the F- ligand
fluoride
-
fluoride coordinates to the heme iron in Cld exhibiting ny(FeIII-F) band at 385 per cm. Strong H-bond donation happens to the F- ligand
additional information
-
no product inhibition by O2 or chloride at millimolar concentrations
-
additional information
-
suicide inactivation by oxidative heme destruction
-
additional information
Stutzerimonas chloritidismutans
-
excess chlorite inactivates and bleaches the enzyme, 80% activity loss with 56 mM chlorite, 90% after second application of 56 mM chlorite; no inhibition by hydroxylamine or 3-amino-1,2,3-triazole
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
presence of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) modestly increases turnover number
2-chloro-5,5-dimethyl-1,3-cyclohexanedione
-
presence of 2-chloro-5,5-dimethyl-1,3-cyclohexanedione modestly increases turnover number
additional information
presence of methionine can partly rescue inactivation during the reaction
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.057
Chlorite