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Literature summary for 1.2.5.3 extracted from

  • Pelzmann, A.; Mickoleit, F.; Meyer, O.
    Insights into the posttranslational assembly of the Mo-, S- and Cu-containing cluster in the active site of CO dehydrogenase of Oligotropha carboxidovorans (2014), J. Biol. Inorg. Chem., 19, 1399-1414.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information metal cluster composition, structure and function of CO dehydrogenase synthesized in mutants of Oligotropha carboxidovorans strain OM5 in which the genes coxE, coxF and coxG are disrupted by insertional mutagenesis, recombinant expression in Escherichia coli strain S17-1, overview. Mutants in coxG retain the ability to utilize CO, although at a lower growth rate. They contain a regular CO dehydrogenase with a functional catalytic site. The CoxD protein is a distinct AAA+ ATPase. CoxD operates in the maturation of the CO dehydrogenase bimetallic cluster, particularly in the sulfuration of the [MoO3]-site and in ATP-dependent chaperone function. Disruption of coxD leads to a phenotype of D-km which is impaired in the utilization of CO, whereas the utilization of H2 plus CO2 is not affected. Under appropriate induction conditions, bacteria synthesize a fully assembled apo-CO dehydrogenase, which cannot oxidize CO. Apo-CO dehydrogenase contained a [MoO3] site in place of the [CuSMoO2] clusters. The genes coxE and coxF are both obligatory for the utilization of CO as a growth substrate Afipia carboxidovorans

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane role of the pleckstrin homology domain of enzyme CoxG in recruiting CO dehydrogenase to the cytoplasmic membrane enabling electron transfer from the enzyme to the respiratory chain Afipia carboxidovorans 16020
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Metals/Ions

Metals/Ions Comment Organism Structure
copper bimetallic [CuSMoO2] cluster Afipia carboxidovorans
Fe2+ iron-sulfur cluster Afipia carboxidovorans
Molybdenum bimetallic [CuSMoO2] cluster Afipia carboxidovorans
[CuSMoO2] cluster CO oxidation by CO dehydrogenase proceeds at a unique [Mo+VIO2-S-Cu+I-S-Cys] cluster which matures posttranslationally while integrated into the completely folded apoenzyme. The Mo ion of the cluster is coordinated by the ene-dithiolate of the molybdopterin cytosine dinucleotide cofactor (MCD). The cofactor biosynthesis starts with the MgATP-dependent, reductive sulfuration of [MoVIO3] to [MoVO2SH] which entails the AAA+-ATPase chaperone CoxD. Then MoV is reoxidized and Cu1+-ion is integrated. Copper is supplied by the soluble CoxF protein which forms a complex with the membrane-bound von Willebrand protein CoxE through RGD-integrin interactions and enables the reduction of CoxF-bound Cu2+, employing electrons from respiration. Copper appears as Cu2+-phytate, is mobilized through the phytase activity of CoxF and then transferred to the CoxF putative copperbinding site. The coxG gene does not participate in the maturation of the bimetallic cluster Afipia carboxidovorans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Afipia carboxidovorans 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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Organism

Organism UniProt Comment Textmining
Afipia carboxidovorans
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
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Subunits

Subunits Comment Organism
heterohexamer
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Afipia carboxidovorans

Cofactor

Cofactor Comment Organism Structure
FAD
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Afipia carboxidovorans
additional information the enzyme is a molybdo iron-sulfur flavoprotein Afipia carboxidovorans
[CuSMoO2] cluster CO oxidation by CO dehydrogenase proceeds at a unique [Mo+VIO2-S-Cu+I-S-Cys] cluster which matures posttranslationally while integrated into the completely folded apoenzyme. The Mo ion of the cluster is coordinated by the ene-dithiolate of the molybdopterin cytosine dinucleotide cofactor (MCD). The cofactor biosynthesis starts with the MgATP-dependent, reductive sulfuration of [MoVIO3] to [MoVO2SH] which entails the AAA+-ATPase chaperone CoxD. Then MoV is reoxidized and Cu1+-ion is integrated. Copper is supplied by the soluble CoxF protein which forms a complex with the membrane-bound von Willebrand protein CoxE through RGD-integrin interactions and enables the reduction of CoxF-bound Cu2+, employing electrons from respiration. Copper appears as Cu2+-phytate, is mobilized through the phytase activity of CoxF and then transferred to the CoxF putative copperbinding site. The coxG gene does not participate in the maturation of the bimetallic cluster Afipia carboxidovorans

General Information

General Information Comment Organism
evolution the enzyme belongs to the molybdenum hydroxylase (xanthine oxidase) family of Mo enzymes Afipia carboxidovorans
malfunction metal cluster composition, structure and function of CO dehydrogenase synthesized in mutants of Oligotropha carboxidovorans strain OM5 in which the genes coxE, coxF and coxG are disrupted by insertional mutagenesis, recombinant expression in Escherichia coli strain S17-1, overview. Mutants in coxG retain the ability to utilize CO, although at a lower growth rate. They contain a regular CO dehydrogenase with a functional catalytic site. Disruption of coxD leads to a phenotype of D-km which is impaired in the utilization of CO, whereas the utilization of H2 plus CO2 is not affected. The deletion of coxG leads to a phenotype which is still able to utilize CO, although the generation time increases considerably from 21 h (wild-type) to 149 h. Under appropriate induction conditions, bacteria synthesize a fully assembled apo-CO dehydrogenase, which cannot oxidize CO. Apo-CO dehydrogenase contains a [MoO3] site in place of the [CuSMoO2] clusters Afipia carboxidovorans
metabolism the CoxD protein is a distinct AAA+ ATPase. CoxD operates in the maturation of the CO dehydrogenase bimetallic cluster, particularly in the sulfuration of the [MoO3]-site and in ATP-dependent chaperone function. The genes coxE and coxF are both obligatory for the utilization of CO as a growth substrate Afipia carboxidovorans
physiological function carbon monoxide dehydrogenases are key to the generation of a proton motive force across the cytoplasmic membrane for ATP synthesis or cooperate with acetyl-CoA synthase in the biosynthesis of acetyl-CoA Afipia carboxidovorans