1.2.5.3: aerobic carbon monoxide dehydrogenase
This is an abbreviated version!
For detailed information about aerobic carbon monoxide dehydrogenase, go to the full flat file.
Word Map on EC 1.2.5.3
Reaction
Synonyms
aerobic Mo/Cu-containing CO dehydrogenase, Carbon monoxide dehydrogenase, CO dehydrogenase, CODH, CoxS, coxSML, CutL, CutM, CutS, EC 1.2.2.4, EC 1.2.3.10, Mo-CODH, Mo-Cu carbon monoxide dehydrogenase, Mo/Cu CODH, MoCu-CODH, molybdenum- and copper-containing carbon monoxide dehydrogenase, molybdenum- and copper-dependent CO dehydrogenase, molybdenum-containing carbon monoxide dehydrogenase, molybdenum-containing CO dehydrogenase, molybdenum-copper carbon monoxide dehydrogenase, molybdenum-copper CO dehydrogenase, molybdenum/copper-containing carbon monoxide dehydrogenase, molybdoenzyme carbon monoxide dehydrogenase
ECTree
1.2.5.3 aerobic carbon monoxide dehydrogenaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.2.5.3 - aerobic carbon monoxide dehydrogenase
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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
CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
CO2 + 1,2-naphthoquinol-4-sulfonic acid
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-
-
-
-
?
CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
CO2 + 1,2-naphthoquinol-4-sulfonic acid
-
-
-
?
CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
CO2 + 1,2-naphthoquinol-4-sulfonic acid
Afipia carboxidovorans ATCC 49405
-
-
-
?
CO + 1,4-naphthoquinone + H2O
CO2 + 1,4-naphthoquinol
-
-
-
?
CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
?
CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
?
CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
?
CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
?
CO + a quinone + H2O
CO2 + a quinol
-
-
-
?
CO + a quinone + H2O
CO2 + a quinol
-
the enzyme catalyzes the oxidation of CO to CO2, yielding two electrons and two H+
-
-
?
CO + a quinone + H2O
CO2 + a quinol
-
-
-
?
CO + benzoquinone + H2O
CO2 + benzoquinol
-
-
-
?
CO + methyl viologen + H2O
CO2 + reduced methylene blue
methyl viologen as an electron acceptor and saturated carbon monoxide as an electron donor
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-
?
CO + methyl viologen + H2O
CO2 + reduced methylene blue
methyl viologen as an electron acceptor and saturated carbon monoxide as an electron donor
-
-
?
CO + methylene blue + H2O
CO2 + NAD+
methyl blue as an electron acceptor and saturated carbon monoxide as an electron donor
-
-
?
CO + methylene blue + H2O
CO2 + NAD+
methyl blue as an electron acceptor and saturated carbon monoxide as an electron donor
-
-
?
CO + NADPH + H+ + H2O
CO2 + reduced methyl viologen
-
-
-
?
CO + NADPH + H+ + H2O
CO2 + reduced methyl viologen
-
-
-
?
CO + ubiquinone + H2O
CO2 + ubiquinol
ubiquinone is the likely physiological oxidant for CO dehydrogenase
-
-
?
CO + ubiquinone + H2O
CO2 + ubiquinol
oxidation of carbon monoxide occurs at the binuclear center with reducing equivalents passed from the redox-active molybdenum to the proximal Fe-S cluster I to the distal Fe-S cluster II and finally to the FAD cofactor
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-
?
additional information
?
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-
routine activity is determined by the CO-dependent reduction of methylene blue. No activity with cytochrome b561. Quinone substrates interacted with CODH at its FAD site
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-
?
additional information
?
-
air-stable CO dehydrogenase having a binuclear molybdenum- and copper-containing active site catalyzes the first step in this process, the oxidation of CO to CO2, with the reducing equivalents. Enzyme reduction and reactivity with H2, kinetics, overview
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-
?
additional information
?
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-
air-stable CO dehydrogenase having a binuclear molybdenum- and copper-containing active site catalyzes the first step in this process, the oxidation of CO to CO2, with the reducing equivalents. Enzyme reduction and reactivity with H2, kinetics, overview
-
-
?
additional information
?
-
-
carbon monoxide dehydrogenases (CO dehydrogenases) are enzymes which catalyze the oxidation of CO to CO2 yielding two electrons and two protons (CO + H2O = CO2 + 2e- + 2H+) or the reverse reaction. CO oxidation by CO dehydrogenase proceeds at a unique bimetallic [CuSMoO2] cluster which matures posttranslationally while integrated into the completely folded apoenzyme
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-
?
additional information
?
-
analysis of mechanism of H2 oxidation, which involves initial binding of H2 to the copper of the binuclear center, displacing the bound water, followed by sequential deprotonation through a copper-hydride intermediate to reduce the binuclear center.The enzyme can be reduced by H2 with a limiting rate constant of 5.3/s and a dissociation constant Kd of 0.525 mM, steady-state and stopped-flow rapid reaction kinetics, overview
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-
?
additional information
?
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-
analysis of mechanism of H2 oxidation, which involves initial binding of H2 to the copper of the binuclear center, displacing the bound water, followed by sequential deprotonation through a copper-hydride intermediate to reduce the binuclear center.The enzyme can be reduced by H2 with a limiting rate constant of 5.3/s and a dissociation constant Kd of 0.525 mM, steady-state and stopped-flow rapid reaction kinetics, overview
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-
?
additional information
?
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-
quinones are unusual physiological oxidants for this family of enzymes
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?
additional information
?
-
the CO dehydrogenation reaction requires the oxidized state of the enzyme. The oxidation of CO mediated by CO dehydrogenase is followed spectrophotometrically with 1-phenyl-2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride/1-methoxyphenazine methosulfate as artificial electron acceptors. Oxidation of xanthine by CO dehydrogenase
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-
?
additional information
?
-
is able to catalyze both the oxidation of CO to CO2 and the oxidation of H2 to protons and electrons
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-
additional information
?
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is able to catalyze both the oxidation of CO to CO2 and the oxidation of H2 to protons and electrons
-
-
-
additional information
?
-
Afipia carboxidovorans ATCC 49405
routine activity is determined by the CO-dependent reduction of methylene blue. No activity with cytochrome b561. Quinone substrates interacted with CODH at its FAD site
-
-
?
additional information
?
-
the CO dehydrogenation reaction requires the oxidized state of the enzyme. The oxidation of CO mediated by CO dehydrogenase is followed spectrophotometrically with 1-phenyl-2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride/1-methoxyphenazine methosulfate as artificial electron acceptors. Oxidation of xanthine by CO dehydrogenase
-
-
?
additional information
?
-
is able to catalyze both the oxidation of CO to CO2 and the oxidation of H2 to protons and electrons
-
-
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