1.2.5.3 CO + 1,2-naphthoquinone-4-sulfonic acid + H2O - Afipia carboxidovorans CO2 + 1,2-naphthoquinol-4-sulfonic acid - ? 435403 1.2.5.3 CO + 1,2-naphthoquinone-4-sulfonic acid + H2O - - CO2 + 1,2-naphthoquinol-4-sulfonic acid - ? 435403 1.2.5.3 CO + 1,2-naphthoquinone-4-sulfonic acid + H2O - Afipia carboxidovorans ATCC 49405 CO2 + 1,2-naphthoquinol-4-sulfonic acid - ? 435403 1.2.5.3 CO + 1,4-naphthoquinone + H2O - Afipia carboxidovorans CO2 + 1,4-naphthoquinol - ? 435404 1.2.5.3 CO + 1,4-naphthoquinone + H2O - - CO2 + 1,4-naphthoquinol - ? 435404 1.2.5.3 CO + 1,4-naphthoquinone + H2O - Afipia carboxidovorans ATCC 49405 CO2 + 1,4-naphthoquinol - ? 435404 1.2.5.3 CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O - Hydrogenophaga pseudoflava CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride - ? 435405 1.2.5.3 CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O - Afipia carboxidovorans CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride - ? 435405 1.2.5.3 CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O - Afipia carboxidovorans DSM 1227 CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride - ? 435405 1.2.5.3 CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O - Hydrogenophaga pseudoflava DSM 1084 CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride - ? 435405 1.2.5.3 CO + a quinone + H2O - Afipia carboxidovorans CO2 + a quinol - ? 434636 1.2.5.3 CO + a quinone + H2O - Hydrogenophaga pseudoflava CO2 + a quinol - ? 434636 1.2.5.3 CO + a quinone + H2O - - CO2 + a quinol - ? 434636 1.2.5.3 CO + a quinone + H2O the enzyme catalyzes the oxidation of CO to CO2, yielding two electrons and two H+ Afipia carboxidovorans CO2 + a quinol - ? 434636 1.2.5.3 CO + a quinone + H2O - Afipia carboxidovorans ATCC 49405 CO2 + a quinol - ? 434636 1.2.5.3 CO + a quinone + H2O - Hydrogenophaga pseudoflava DSM 1084 CO2 + a quinol - ? 434636 1.2.5.3 CO + benzoquinone + H2O - Afipia carboxidovorans CO2 + benzoquinol - ? 435406 1.2.5.3 CO + benzoquinone + H2O - - CO2 + benzoquinol - ? 435406 1.2.5.3 CO + benzoquinone + H2O - Afipia carboxidovorans ATCC 49405 CO2 + benzoquinol - ? 435406 1.2.5.3 CO + methyl viologen + H2O methyl viologen as an electron acceptor and saturated carbon monoxide as an electron donor Aeropyrum pernix CO2 + reduced methylene blue - ? 435407 1.2.5.3 CO + methyl viologen + H2O methyl viologen as an electron acceptor and saturated carbon monoxide as an electron donor Aeropyrum pernix TB5 CO2 + reduced methylene blue - ? 435407 1.2.5.3 CO + methylene blue + H2O methyl blue as an electron acceptor and saturated carbon monoxide as an electron donor Aeropyrum pernix CO2 + NAD+ - ? 435408 1.2.5.3 CO + methylene blue + H2O methyl blue as an electron acceptor and saturated carbon monoxide as an electron donor Aeropyrum pernix TB5 CO2 + NAD+ - ? 435408 1.2.5.3 CO + NADH + H+ + H2O - Aeropyrum pernix CO2 + NADP+ - ? 435409 1.2.5.3 CO + NADH + H+ + H2O - Aeropyrum pernix TB5 CO2 + NADP+ - ? 435409 1.2.5.3 CO + NADPH + H+ + H2O - Aeropyrum pernix CO2 + reduced methyl viologen - ? 435410 1.2.5.3 CO + NADPH + H+ + H2O - Aeropyrum pernix TB5 CO2 + reduced methyl viologen - ? 435410 1.2.5.3 CO + ubiquinone + H2O - Afipia carboxidovorans CO2 + ubiquinol - ? 434637 1.2.5.3 CO + ubiquinone + H2O ubiquinone is the likely physiological oxidant for CO dehydrogenase Afipia carboxidovorans CO2 + ubiquinol - ? 434637 1.2.5.3 CO + ubiquinone + H2O 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 Afipia carboxidovorans CO2 + ubiquinol - ? 434637 1.2.5.3 CO + ubiquinone-1 + H2O - - CO2 + ubiquinol-1 - ? 435411 1.2.5.3 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 Afipia carboxidovorans ? - ? 89 1.2.5.3 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 Afipia carboxidovorans ? - ? 89 1.2.5.3 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 Afipia carboxidovorans ? - ? 89 1.2.5.3 additional information quinones are unusual physiological oxidants for this family of enzymes Afipia carboxidovorans ? - ? 89 1.2.5.3 additional information 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 - ? - ? 89 1.2.5.3 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 Afipia carboxidovorans ? - ? 89 1.2.5.3 additional information is able to catalyze both the oxidation of CO to CO2 and the oxidation of H2 to protons and electrons Afipia carboxidovorans ? - - 89 1.2.5.3 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 Afipia carboxidovorans DSM 1227 ? - ? 89 1.2.5.3 additional information is able to catalyze both the oxidation of CO to CO2 and the oxidation of H2 to protons and electrons Afipia carboxidovorans DSM 1227 ? - - 89 1.2.5.3 additional information 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 Afipia carboxidovorans ATCC 49405 ? - ? 89