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Literature summary extracted from

  • Hille, R.; Dingwall, S.; Wilcoxen, J.
    The aerobic CO dehydrogenase from Oligotropha carboxidovorans (2015), J. Biol. Inorg. Chem., 20, 243-251.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.5.3 the enzyme is encoded by the coxMSL structural genes in the megaplasmid-localized coxBCMSLDEFGHIK gene cluster Afipia carboxidovorans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.5.3 enzyme in complex with inhibitor n-butylisonitrile, PDB ID 1N62, structure analysis Afipia carboxidovorans

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.5.3 additional information thiol inhibition of CO dehydrogenase Afipia carboxidovorans
1.2.5.3 n-butylisonitrile
-
 Afipia carboxidovorans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.2.5.3 membrane the enzyme's physiological position is on the inner side of the cytoplasmic membrane, membrane associated, if not membrane-integral Afipia carboxidovorans 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.5.3 Fe2+
-
 Afipia carboxidovorans
1.2.5.3 Molybdenum
-
 Afipia carboxidovorans
1.2.5.3 [2Fe-2S] cluster two [2Fe-2S] iron-sulfur clusters in the small subunit Afipia carboxidovorans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.5.3 CO + ubiquinone + H2O Afipia carboxidovorans ubiquinone is the likely physiological oxidant for CO dehydrogenase CO2 + ubiquinol
-
 ?
1.2.5.3 additional information Afipia carboxidovorans 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 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.5.3 Afipia carboxidovorans P19919 and P19920 and P19921 genes coxL, coxM, and coxS; the enzyme is encoded by coxMSL structural genes in the megaplasmid-localized coxBCMSLDEFGHIK gene cluster
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.2.5.3 CO + a quinone + H2O = CO2 + a quinol proposed reaction mechanisms for CO dehydrogenase, the rate-limiting step for overall turnover resides in the reductive half-reaction, reoxidation of reduced enzyme by quinones occurs at the FAD site Afipia carboxidovorans
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.5.3 CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
-
 Afipia carboxidovorans CO2 + 1,2-naphthoquinol-4-sulfonic acid
-
 ?
1.2.5.3 CO + 1,4-naphthoquinone + H2O
-
 Afipia carboxidovorans CO2 + 1,4-naphthoquinol
-
 ?
1.2.5.3 CO + a quinone + H2O
-
 Afipia carboxidovorans CO2 + a quinol
-
 ?
1.2.5.3 CO + benzoquinone + H2O
-
 Afipia carboxidovorans CO2 + benzoquinol
-
 ?
1.2.5.3 CO + ubiquinone + H2O ubiquinone is the likely physiological oxidant for CO dehydrogenase Afipia carboxidovorans CO2 + ubiquinol
-
 ?
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 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.5.3 heterohexamer (abc)2 structure, each protomer of the enzyme has a small subunit (CoxS, 18 kDa) with two [2Fe-2S] iron-sulfur clusters, a medium subunit (CoxM, 30 kDa) that possesses FAD, and a large subunit (CoxL, 89 kDa) that has the active site binuclear center Afipia carboxidovorans

Synonyms

EC Number Synonyms Comment Organism
1.2.5.3 aerobic Mo/Cu-containing CO dehydrogenase
-
 Afipia carboxidovorans
1.2.5.3 molybdenum- and copper-dependent CO dehydrogenase
-
 Afipia carboxidovorans

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.5.3 benzoquinone
-
 Afipia carboxidovorans
1.2.5.3 FAD located in the medium subunit Afipia carboxidovorans
1.2.5.3 molybdopterin cofactor the structure of the active site binuclear center of CO dehydrogenase in its oxidized form, overview. The oxidized Mo(VI) ion has the distorted square-pyramidal coordination geometry seen in other members of the xanthine oxidase family of molybdenum-containing enzymes, with an apical Mo=O and an equatorial plane consisting of a second Mo=O group rather than the catalytically labile Mo-OH seen in other family members and two sulfurs from a pyranopterin cofactor that is common to all molybdenum and tungsten enzymes. The pyranopterin cofactor is present as the dinucleotide of cytosine Afipia carboxidovorans
1.2.5.3 quinone quinone cofactors interact with CODH at its FAD site Afipia carboxidovorans
1.2.5.3 ubiquinone-1
-
 Afipia carboxidovorans

General Information

EC Number General Information Comment Organism
1.2.5.3 evolution despite the unique nature of the binuclear active site of CO dehydrogenase the enzyme is clearly a member of the xanthine oxidase family of molybdenum-containing enzymes Afipia carboxidovorans
1.2.5.3 malfunction thiol inhibition of CO dehydrogenase may be a physiologically important mechanism of enzyme regulation Afipia carboxidovorans
1.2.5.3 metabolism four other genes (coxB, coxC, coxH and coxK) are predicted to encode proteins possessing one (CoxB) to as many as nine (CoxK) transmembrane helices, one or more of which are likely to be involved in anchoring CO dehydrogenase to its physiological position on the inner side of the cytoplasmic membrane Afipia carboxidovorans
1.2.5.3 additional information the enzyme possesses a deeply buried binuclear center of CO dehydrogenase activity Afipia carboxidovorans