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Literature summary for 1.2.5.3 extracted from

  • Wilcoxen, J.; Zhang, B.; Hille, R.
    Reaction of the molybdenum- and copper-containing carbon monoxide dehydrogenase from Oligotropha carboxydovorans with quinones (2011), Biochemistry, 50, 1910-1916.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.5.3

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CO + a quinone + H2O
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-
 CO2 + a quinol
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 ?
CO + a quinone + H2O Afipia carboxidovorans ATCC 49405
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 CO2 + a quinol
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 ?

Organism

Organism UniProt Comment Textmining
Afipia carboxidovorans ATCC 49405 P19919 AND P19920 AND P19921 genes coxL, coxM, and coxS; genes coxS, coxM, and coxL
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
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-
 CO2 + 1,2-naphthoquinol-4-sulfonic acid
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 ?
CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
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 Afipia carboxidovorans ATCC 49405 CO2 + 1,2-naphthoquinol-4-sulfonic acid
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 ?
CO + 1,4-naphthoquinone + H2O
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-
 CO2 + 1,4-naphthoquinol
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 ?
CO + 1,4-naphthoquinone + H2O
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 Afipia carboxidovorans ATCC 49405 CO2 + 1,4-naphthoquinol
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 ?
CO + a quinone + H2O
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-
 CO2 + a quinol
-
 ?
CO + a quinone + H2O
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 Afipia carboxidovorans ATCC 49405 CO2 + a quinol
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 ?
CO + benzoquinone + H2O
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 CO2 + benzoquinol
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 ?
CO + benzoquinone + H2O
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 Afipia carboxidovorans ATCC 49405 CO2 + benzoquinol
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 ?
CO + ubiquinone-1 + H2O
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 CO2 + ubiquinol-1
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 ?
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
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 ?
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 ?
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 ?
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 ?

Subunits

Subunits Comment Organism
heterohexamer the functional enzyme is a (alphabetagamma)2 hexamer that consists of a small 17.8 kDa subunit (CoxS) containing two [2Fe-2S] clusters, a medium 30.2 kDa subunit (CoxM) containing an FAD cofactor, and a large 88.7 kDa subunit (CoxL) that possesses the molybdenum center
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Synonyms

Synonyms Comment Organism
Carbon monoxide dehydrogenase
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CODH
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molybdenum- and copper-containing carbon monoxide dehydrogenase
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General Information

General Information Comment Organism
evolution the enzyme belongs to the XOR family
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physiological function carbon monoxide dehydrogenase from Oligotropha carboxydovorans catalyzes the oxidation of carbon monoxide to carbon dioxide, providing the organism both a carbon source and energy for growth. In the oxidative half of the catalytic cycle, electrons gained from CO are ultimately passed to the electron transport chain of the Gram-negative organism. Quinones are catalytically competent as proximal acceptor of reducing equivalents from the enzyme
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