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Literature summary for 1.2.5.3 extracted from

  • Resch, M.; Dobbek, H.; Meyer, O.
    Structural and functional reconstruction in situ of the [CuSMoO 2] active site of carbon monoxide dehydrogenase from the carbon monoxide oxidizing eubacterium Oligotropha carboxidovorans (2005), J. Biol. Inorg. Chem., 10, 518-528.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
purified reconstituted enzyme, hangig drop vapour diffusion method, X-ray diffraction structure determination and analysis at 1.7 A resolution Afipia carboxidovorans

Metals/Ions

Metals/Ions Comment Organism Structure
copper essential, in the [CuSMoO2] cluster Afipia carboxidovorans
Fe2+ in two [2Fe-2S] clusters Afipia carboxidovorans
Molybdenum essential, in the [CuSMoO2] cluster Afipia carboxidovorans
additional information the removal of Cu and S from the active site changes the functional [CuSMoO2] centre into a non-functional [MoO3] centre. The insertion of a sulfur atom from sodium sulfide into the [MoO3] center yielding a [MoO2S] center. The latter does not catalyze the oxidation of CO referring to a nonfunctional Mo-centre. Resulfuration of the [MoO3] centre and transfer of Cu from the Cu(I)–thiourea complex to the [MoO2S] centre partially restores the specific CO oxidizing activity Afipia carboxidovorans
[2Fe-2S] cluster a type I and a type II [2Fe-2S] center. The iron-sulfur protein carries the two [2Fe-2S] clusters, which can be distinguished by electron paramagnetic resonance spectroscopy Afipia carboxidovorans
[CuSMoO2] cluster the Mo-ion in the oxidized cluster is in +VI oxidation state and upon incubation with CO or sodium dithionite is reduced to Mo(IV). The Cu ion permanently remains in the +1 oxidation state. The ligands around Mo form a distorted square pyramidal geometry. The large subunit forms a molybdoprotein Afipia carboxidovorans

Organism

Organism UniProt Comment Textmining
Afipia carboxidovorans P19919 and P19920 and P19921 genes coxL, coxM, and coxS; formerly Pseudomonas carboxydovorans strain OM5, genes coxS, coxM, and coxL encoded on the low-copy-number 133,058 bp-circular DNA megaplasmid pHCG3
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Afipia carboxidovorans DSM 1227 P19919 and P19920 and P19921 genes coxL, coxM, and coxS; formerly Pseudomonas carboxydovorans strain OM5, genes coxS, coxM, and coxL encoded on the low-copy-number 133,058 bp-circular DNA megaplasmid pHCG3
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Renatured (Commentary)

Renatured (Comment) Organism
reconstitution of 50% enzyme activity by in vitro reconstitution of the active site through the supply of sulfide first and subsequently of Cu(I) under reducing conditions. Immature forms of CO dehydrogenase isolated from the bacterium, which are deficient in S and/or Cu at the active site, are similarly activated. The [CuSMoO2] cluster is properly reconstructed Afipia carboxidovorans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
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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 Afipia carboxidovorans DSM 1227 ?
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 ?

Subunits

Subunits Comment Organism
heterohexamer CO dehydrogenase is composed of a 88.7 kDa molybdoprotein (L subunit), a 30.2 kDa flavoprotein (M subunit), and a 17.8 kDa iron-sulfur protein (S subunit) in a (LMS)2 subunit composition Afipia carboxidovorans

Synonyms

Synonyms Comment Organism
Carbon monoxide dehydrogenase
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 Afipia carboxidovorans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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 assay at, reconstituted enzyme Afipia carboxidovorans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.2
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 assay at, reconstituted enzyme Afipia carboxidovorans

Cofactor

Cofactor Comment Organism Structure
FAD FAD is bound in the medium subunit, a flavoprotein Afipia carboxidovorans
additional information rescue of 50% enzyme activity by in vitro reconstitution of the active site through the supply of sulfide first and subsequently of Cu(I) under reducing conditions. Immature forms of CO dehydrogenase isolated from the bacterium, which are deficient in S and/or Cu at the active site, are similarly activated. The [CuSMoO2] cluster is properly reconstructed. Sulfane sulfur is bound in the active site of CO dehydrogenase. Rebuilding a functional [CuSMoO2] centre by first generating a [MoO3] centre in the active site of CO dehydrogenase Afipia carboxidovorans

General Information

General Information Comment Organism
malfunction the removal of Cu and S from the active site changes the functional [CuSMoO2] centre into a non-functional [MoO3] centre Afipia carboxidovorans