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.
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
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Substrates Products
Substrates Products on EC 1.2.5.3 - aerobic carbon monoxide dehydrogenase
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REACTION DIAGRAM
CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
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
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CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
CO2 + 1,2-naphthoquinol-4-sulfonic acid
Afipia carboxidovorans ATCC 49405
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CO + 1,4-naphthoquinone + H2O
CO2 + 1,4-naphthoquinol
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CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
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CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
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CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
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CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
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CO + a quinone + H2O
CO2 + a quinol
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CO + a quinone + H2O
CO2 + a quinol
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the enzyme catalyzes the oxidation of CO to CO2, yielding two electrons and two H+
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CO + a quinone + H2O
CO2 + a quinol
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CO + benzoquinone + H2O
CO2 + benzoquinol
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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
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CO2 + NAD+
methyl blue as an electron acceptor and saturated carbon monoxide as an electron donor
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CO + methylene blue + H2O
CO2 + NAD+
methyl blue as an electron acceptor and saturated carbon monoxide as an electron donor
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CO2 + reduced methyl viologen
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CO + NADPH + H+ + H2O
CO2 + reduced methyl viologen
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CO + ubiquinone + H2O
CO2 + ubiquinol
ubiquinone is the likely physiological oxidant for CO dehydrogenase
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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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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
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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
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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
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additional information
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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
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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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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
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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
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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
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additional information
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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
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additional information
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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
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is able to catalyze both the oxidation of CO to CO2 and the oxidation of H2 to protons and electrons
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