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metabolism
-
the enzyme is the terminal enzyme involved in the perchlorate reduction pathway
evolution

active site conservation and evolution of Cld, overview
evolution
-
The chlorite dismutases (C-family proteins) are a widespread family of heme-binding proteins
evolution
-
The chlorite dismutases (C-family proteins) are a widespread family of heme-binding proteins
-
malfunction

-
the W155F mutation of the enzyme appears to disturb both the relatively higher heme affinity and pentameric oligomerization state common to the wild-type enzyme, mutant W156F, and mutant W227F
malfunction
-
a Staphylococcus aureus strain with an inactivated hemQ gene is generated and shown to be a slow growing small colony variant under aerobic but not anaerobic conditions. The DELTAhemQ mutant accumulates coproporphyrin specifically under aerobic conditions. Phenotypes, overview
malfunction
-
a Staphylococcus aureus strain with an inactivated hemQ gene is generated and shown to be a slow growing small colony variant under aerobic but not anaerobic conditions. The DELTAhemQ mutant accumulates coproporphyrin specifically under aerobic conditions. Phenotypes, overview
-
physiological function

-
the enzyme detoxifies the chlorite that results from chlorate respiration in bacteria and would otherwise accumulate in the cell and kill the organism. The reaction must be fast in order to serve its biological function: the homopentameric enzyme from Dechloromonas aromatica is one of the fastest and most efficient chlorite O2-lyases yet studied. The enzyme can support the generation of tens-of-millimolar O2 on the millisecond timescale
physiological function
-
the enzyme detoxifies the chlorite that results from chlorate respiration in bacteria and would otherwise accumulate in the cell and kill the organism. Nitrobacter has a limited chlorite resistance, which enables it to persist and even oxidize nitrite in the presence of low concentrations of chlorate
physiological function
-
similar substrate role for heme or porphyrin, with possible sensor-regulator functions for the protein
physiological function
-
similar substrate role for heme or porphyrin, with possible sensor-regulator functions for the protein
-
additional information

-
active and inactive enzyme forms dependent on the protonation status, overview
additional information
Candidatus Nitrospira defluvii is a key nitrifier in biological wastewater treatment, molecular mechanism of chlorite detoxification, overview. The residue corresponding to Arg173 is conserved in all known active forms of Cld and propose it as a marker for Cld activity in yet uncharacterized Cld-like proteins
additional information
-
the enzyme is capable of approximately 17000 turnovers per heme before undergoing irreversible inactivation due to oxidative damage to the heme
additional information
-
conformational and thermal stability of recombinant dimeric Cld from Nitrobacter winogradskyi, overview
additional information
-
conformational and thermal stability of recombinant pentameric Cld from Nitrospira defluvii, overview
additional information
-
despite a truncated N-terminal domain in each subunit, the dimeric enzyme is a highly efficient chlorite dismutase. Subunit interface and active site structures, structure modeling, overview
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additional information
?
-
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
-
-
-
-
ir
chlorite
chloride + O2
-
-
-
-
?
chlorite
chloride + O2
-
-
-
-
ir
chlorite
chloride + O2
catalytic mechanism via ferryl species and ClO--anion
-
-
?
chlorite
chloride + O2
-
-
-
-
?
chlorite
chloride + O2
-
-
-
-
ir
chlorite
chloride + O2
catalytic mechanism via ferryl species and ClO--anion
-
-
?
chlorite
chloride + O2
-
-
-
?
chlorite
chloride + O2
Bacteria GR-1
-
-
-
?
chlorite
chloride + O2
-
-
-
-
ir
chlorite
chloride + O2
-
-
-
-
?
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
-
-
-
-
?
chlorite
chloride + O2
-
-
-
-
?
chlorite
chloride + O2
Dechlorosoma sp.
-
-
-
-
?
chlorite
chloride + O2
-
-
-
-
?
chlorite
chloride + O2
-
-
-
?
chlorite
chloride + O2
-
-
-
?
chlorite
chloride + O2
-
-
-
-
?
chlorite
chloride + O2
-
-
-
-
?
chlorite
chloride + O2
-
-
-
-
ir
chlorite
chloride + O2
-
-
degradation of n-alkane or intermediates + chlorate
-
?
chlorite
chloride + O2
-
-
water is not involved in the O2-building reaction (no inclusion of 18O-isotope from labeled water)
-
?
chlorite
chloride + O2
-
-
degradation of n-alkane or intermediates + chlorate
-
?
chlorite
chloride + O2
-
-
water is not involved in the O2-building reaction (no inclusion of 18O-isotope from labeled water)
-
?
chlorite
chloride + O2
-
-
degradation of n-alkane or intermediates + chlorate
-
?
chlorite
chloride + O2
-
-
-
-
?
chlorite
chloride + O2
-
-
-
-
?
chlorite
chloride + O2
-
-
-
-
?
additional information

?
-
-
PitA possesses both chlorite dismutase-related (N-terminus) and antibiotic biosynthesis monooxygenase-related (C-terminus) activities
-
-
-
additional information
?
-
-
PitA possesses both chlorite dismutase-related (N-terminus) and antibiotic biosynthesis monooxygenase-related (C-terminus) activities
-
-
-
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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dimer
-
conformational and thermal stability of recombinant dimeric Cld from Nitrobacter winogradskyi, overview
additional information
-
the Cld-like protein from the chemolithoautotrophic nitrite oxidizer Nitrobacter winogradskyi is significantly smaller than all previously known chlorite dismutases
?

-
x * 32000, SDS-PAGE
?
Bacteria GR-1
-
x * 32000, SDS-PAGE
-
hexamer

6 * 30000, multiple anomalous dispersion crystal structure, one heme per monomer (histidine 170 axial heme ligand), arginine 183 probably with essential role in substrate positioning and activation, activity of the hexamer not measurable because of the presence of the thiocyanate inhibitor, each monomer appears to be acting on its own, therefore, different quaternary states may be biologically relevant depending on protein concentration, pH, or other factors
hexamer
-
6 * 30000, multiple anomalous dispersion crystal structure, one heme per monomer (histidine 170 axial heme ligand), arginine 183 probably with essential role in substrate positioning and activation, activity of the hexamer not measurable because of the presence of the thiocyanate inhibitor, each monomer appears to be acting on its own, therefore, different quaternary states may be biologically relevant depending on protein concentration, pH, or other factors
-
homodimer

-
2 * 28400, recombinant mutant W155F, SDS-PAGE
homodimer
-
subunit interface and active site structures, structure modeling, overview
homopentamer

-
-
homopentamer
each monomer of NdCld is characterized by two topologically equivalent four-stranded antiparallel beta-sheets forming a beta-barrel, flanked on both sides by six alpha-helices, overview
homotetramer

-
4 * 31000, heme content 1.5 mol Fe2+/mol enzyme (calculated from Soret peak shift measurement), 2.2 mol Fe2+/mol enzyme (metal analysis by ICP-MS)
homotetramer
-
4 * 31000, heme content 1.5 mol Fe2+/mol enzyme (calculated from Soret peak shift measurement), 2.2 mol Fe2+/mol enzyme (metal analysis by ICP-MS)
-
monomer

1 * 30420 without heme, 1 * 31032 with heme
monomer
-
1 * 30420 without heme, 1 * 31032 with heme
-
pentamer

5 * 30000 Da, tandem mass spectrometry, native mass spectrometry, active state in solution
pentamer
-
5 * 30000 Da, tandem mass spectrometry, native mass spectrometry, active state in solution
-
pentamer
-
conformational and thermal stability of recombinant pentameric Cld from Nitrospira defluvii, overview
tetramer

4 * 30000 Da, elution position on a gel-filtration column using Stokes radius to determine molecular weight points to globular tetramer, collisional activation of the ions ejects one monomer of the pentamer, so that low-charged tetramer counter complex ions are also observed with native mass spectrometry
tetramer
-
4 * 30000 Da, elution position on a gel-filtration column using Stokes radius to determine molecular weight points to globular tetramer, collisional activation of the ions ejects one monomer of the pentamer, so that low-charged tetramer counter complex ions are also observed with native mass spectrometry
-
tetramer
-
4 * 28400, SDS-PAGE
tetramer
-
4 * 25000, SDS-PAGE
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Van Ginkel, C.G.; Rikken, G.B.; Kron, A.G.M.; Kengen, S.W.M.
Purification and characterization of chlorite dismutase: a novel oxygen-generating enzyme
Arch. Microbiol.
166
321-326
1996
Bacteria, Bacteria GR-1
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Stenklo, K.; Thorell, H.D.; Bergius, H.; Aasa, R.; Nilsson, T.
Chlorite dismutase from Ideonella dechloratans
J. Biol. Inorg. Chem.
6
601-607
2001
Ideonella dechloratans
brenda
Thorell, H.D.; Karlsson, J.; Portelius, E.; Nilsson, T.
Cloning, characterisation, and expression of a novel gene encoding chlorite dismutase from Ideonella dechloratans
Biochim. Biophys. Acta
1577
445-451
2002
Ideonella dechloratans
brenda
Hagedoorn, P.L.; De Geus, D.C.; Hagen, W.R.
Spectroscopic characterization and ligand-binding properties of chlorite dismutase from the chlorate respiring bacterial strain GR-1
Eur. J. Biochem.
269
4905-4911
2002
Azospira oryzae, Azospira oryzae GR-1
brenda
Thorell, H.D.; Beyer, N.H.; Heegaard, N.H.H.; Oehman, M.; Nilsson, T.
Comparison of native and recombinant chlorite dismutase from Ideonella dechloratans
Eur. J. Biochem.
271
3539-3546
2004
Ideonella dechloratans
brenda
Xu, J.; Logan, B.E.
Measurement of chlorite dismutase activities in perchlorate respiring bacteria
J. Microbiol. Methods
54
239-247
2003
Dechlorosoma sp., Dechlorosoma sp. KJ
brenda
Shrout, J.D.; Scheetz, T.E.; Casavant, T.L.; Parkin, G.F.
Isolation and characterization of autotrophic, hydrogen-utilizing, perchlorate-reducing bacteria
Appl. Microbiol. Biotechnol.
67
261-268
2005
Dechloromonas sp.
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Bab-Dinitz, E.; Shmuely, H.; Maupin-Furlow, J.; Eichler, J.; Shaanan, B.
Haloferax volcanii PitA: an example of functional interaction between the Pfam chlorite dismutase and antibiotic biosynthesis monooxygenase families?
Bioinformatics
22
671-675
2006
Haloferax volcanii, Haloferax volcanii WR341
brenda
de Geus, D.C.; Thomassen, E.A.; van der Feltz, C.L.; Abrahams, J.P.
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of chlorite dismutase: a detoxifying enzyme producing molecular oxygen
Acta Crystallogr. Sect. F
64
730-732
2008
Azospira oryzae, Azospira oryzae GR-1
brenda
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Chemical and steady-state kinetic analyses of a heterologously expressed heme dependent chlorite dismutase
Biochemistry
47
5271-5280
2008
Dechloromonas agitata
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Environmental genomics reveals a functional chlorite dismutase in the nitrite-oxidizing bacterium Candidatus Nitrospira defluvii
Environ. Microbiol.
10
3043-3056
2008
Nitrospira defluvii
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Crystallization and preliminary X-ray diffraction of chlorite dismutase from Dechloromonas aromatica RCB
Acta Crystallogr. Sect. F
65
818-821
2009
Dechloromonas aromatica, Dechloromonas aromatica RCB
brenda
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Isolation and characterization of Alicycliphilus denitrificans strain BC, which grows on benzene with chlorate as the electron acceptor
Appl. Environ. Microbiol.
74
6672-6681
2008
Alicycliphilus denitrificans, Alicycliphilus denitrificans BC, Alicycliphilus sp.
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Growth of Pseudomonas chloritidismutans AW-1(T) on n-alkanes with chlorate as electron acceptor
Appl. Microbiol. Biotechnol.
83
739-747
2009
Pseudomonas chloritidismutans, Pseudomonas chloritidismutans AW-1
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Purification and characterization of a chlorite dismutase from Pseudomonas chloritidismutans
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293
115-121
2009
Pseudomonas chloritidismutans, Pseudomonas chloritidismutans AW-1
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Crystal structure of chlorite dismutase, a detoxifying enzyme producing molecular oxygen
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387
192-206
2009
Azospira oryzae, Azospira oryzae (E2DI02), Azospira oryzae GR-1 (E2DI02)
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Mechanism of and exquisite selectivity for O-O bond formation by the heme-dependent chlorite dismutase
Proc. Natl. Acad. Sci. USA
105
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2008
Dechloromonas aromatica, Dechloromonas aromatica RCB
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How active-site protonation state influences the reactivity and ligation of the heme in chlorite dismutase
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132
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2010
Dechloromonas aromatica
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Structural and functional characterisation of the chlorite dismutase from the nitrite-oxidizing bacterium Candidatus Nitrospira defluvii: identification of a catalytically important amino acid residue
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172
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Nitrospira defluvii (B3U4H7), Nitrospira defluvii
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O2-evolving chlorite dismutase as a tool for studying O2-utilizing enzymes
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51
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2012
Dechloromonas aromatica
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Hofbauer, S.; Gysel, K.; Mlynek, G.; Kostan, J.; Hagmueller, A.; Daims, H.; Furtmueller, P.; Djinovic-Carugo, K.; Obinger, C.
Impact of subunit and oligomeric structure on the thermal and conformational stability of chlorite dismutases
Biochim. Biophys. Acta
1824
1031-1038
2012
Nitrobacter winogradskyi (Q3SPU6), Nitrospira defluvii
brenda
Blanc, B.; Rodgers, K.; Lukat-Rodgers, G.; Dubois, J.
Understanding the roles of strictly conserved tryptophan residues in O2 producing chlorite dismutases
Dalton Trans.
42
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Dechloromonas aromatica
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Kinetics of chlorite dismutase in a perchlorate degrading reactor sludge
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uncultured bacterium
brenda
Mlynek, G.; Sjoeblom, B.; Kostan, J.; Fuereder, S.; Maixner, F.; Gysel, K.; Furtmueller, P.G.; Obinger, C.; Wagner, M.; Daims, H.; Djinovic-Carugo, K.
Unexpected diversity of chlorite dismutases: a catalytically efficient dimeric enzyme from Nitrobacter winogradskyi
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193
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Nitrobacter winogradskyi, Nitrobacter winogradskyi (Q3SPU6)
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23488-23504
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Staphylococcus aureus, Staphylococcus aureus COL
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