1.2.5.3: aerobic carbon monoxide dehydrogenase
This is an abbreviated version!
For detailed information about aerobic carbon monoxide dehydrogenase, go to the full flat file.
Reaction
Synonyms
aerobic Mo/Cu-containing CO dehydrogenase, Carbon monoxide dehydrogenase, CO dehydrogenase, CODH, CoxS, coxSML, CutL, CutM, CutS, EC 1.2.2.4, EC 1.2.3.10, Mo-CODH, Mo-Cu carbon monoxide dehydrogenase, Mo/Cu CODH, MoCu-CODH, molybdenum- and copper-containing carbon monoxide dehydrogenase, molybdenum- and copper-dependent CO dehydrogenase, molybdenum-containing carbon monoxide dehydrogenase, molybdenum-containing CO dehydrogenase, molybdenum-copper carbon monoxide dehydrogenase, molybdenum-copper CO dehydrogenase, molybdenum/copper-containing carbon monoxide dehydrogenase, molybdoenzyme carbon monoxide dehydrogenase
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General Information
General Information on EC 1.2.5.3 - aerobic carbon monoxide dehydrogenase
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evolution
malfunction
metabolism
physiological function
additional information
CO dehydrogenase is a member of the xanthine oxidase family
evolution
CO dehydrogenase is a prototype of the molybdenum hydroxylase sequence family
evolution
CODH enzymes are classified into two groups, Ni-CODH and Mo-CODH, based on the type of metal in the active center. The Ni-CODH active center is constructed from nickel, iron, and sulfur clusters. Ni-CODH is distributed among anaerobic carboxydotrophs. The Mo-CODH active center contains molybdenum. Aerobic carboxydotrophs use Mo-CODH. The CODH protein isolated from Aeropyrum pernix is a distinct type of archaeal Mo-CODH. Phylogenetic analysis, overview
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
evolution
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the enzyme belongs to the molybdenum hydroxylase (xanthine oxidase) family of Mo enzymes
evolution
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the enzyme belongs to the noncanonical members of the xanthine oxidase family. The Mo-containing CO dehydrogenase from Oligotropha carboxidovorans and related organisms is distinct from the highly O2-sensitive Ni/Fe-containing CO dehydrogenase from obligate anaerobes such as Clostridum thermoaceticum or Methanosarcina barkerii. Quinones are unusual physiological oxidants for this family of enzymes, the overall fold of the FAD-containing domain of CO dehydrogenase resembles the dehydrogenase rather than the oxidase form of the bovine xanthine oxidoreductase, particularly with regard to the position of the mobile loop referred to above that is involved in the Dto-O conversion, but there are significant differences in the environment of the FAD in CO dehydrogenase and xanthine dehydrogenase. A Lys-Asp pair near the pyrimidine subnucleus of the flavin is preserved, for example, but the positions of the Ile and aromatic residues are reversed, with the Ile on the re side and Tyr (a Phe in the bovine enzyme) on the si side of the isoalloxazine ring
evolution
the enzyme is a member of the xanthine oxidase (XO) family of pyranopterin molybdenum enzymes that typically catalyse the oxidative hydroxylation of N-heterocyle and aldehyde
evolution
the enzyme is a member of the xanthine oxidase (XO) family of pyranopterin molybdenum enzymes that typically catalyse the oxidative hydroxylation of N-heterocyle and aldehyde substrates
evolution
the Mo- and Cu-containing CO dehydrogenase from Oligotropha carboxydovorans is both mechanistically and structurally distinct from the extremely O2-sensitive Ni- and Fe-containing CO dehydrogenase from organisms such as Moorella thermoacetica or Methanosarcina barkerii. On the basis of overall architecture and sequence homology, the Mo/Cu CO dehydrogenase belongs to the xanthine oxidase family of enzymes but is unique among members of this large and broadly distributed family in several regards: the reaction catalyzed is not formally a hydroxylation reaction involving hydride abstraction from substrate. The enzyme utilizes ubiquinone as the oxidizing substrate rather than O2 or NADas oxidizing substrate, and, most significantly, its unique binuclear active site contains copper as well as molybdenum
evolution
the sequences of CutMSL are highly conserved in CO-DHs and other molybdenum-containing hydroxylases
evolution
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CO dehydrogenase is a prototype of the molybdenum hydroxylase sequence family
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evolution
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CODH enzymes are classified into two groups, Ni-CODH and Mo-CODH, based on the type of metal in the active center. The Ni-CODH active center is constructed from nickel, iron, and sulfur clusters. Ni-CODH is distributed among anaerobic carboxydotrophs. The Mo-CODH active center contains molybdenum. Aerobic carboxydotrophs use Mo-CODH. The CODH protein isolated from Aeropyrum pernix is a distinct type of archaeal Mo-CODH. Phylogenetic analysis, overview
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evolution
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the sequences of CutMSL are highly conserved in CO-DHs and other molybdenum-containing hydroxylases
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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
malfunction
the removal of Cu and S from the active site changes the functional [CuSMoO2] centre into a non-functional [MoO3] centre
malfunction
thiol inhibition of CO dehydrogenase may be a physiologically important mechanism of enzyme regulation
malfunction
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the removal of Cu and S from the active site changes the functional [CuSMoO2] centre into a non-functional [MoO3] centre
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carbon monoxide dehydrogenase (CODH) is a key enzyme of carbon monoxide metabolism in carboxydotrophic bacteria, it catalyzes carbon monoxide oxidation
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
metabolism
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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
metabolism
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the enzyme catalyzes the critical first step in this process, the oxidation of CO to CO2 with the reducing equivalents thus obtained ultimately being passed on ultimately to a CO-insensitive terminal oxidase
metabolism
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carbon monoxide dehydrogenase (CODH) is a key enzyme of carbon monoxide metabolism in carboxydotrophic bacteria, it catalyzes carbon monoxide oxidation
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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
physiological function
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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
physiological function
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Oligotropha carboxidovorans is a carboxydotrophic bacterium capable of aerobic, chemolithoautotrophic growth using COas a sole source of carbon and energy. The key enzyme involved in this facultative metabolism is an air-stable molybdenum-containing CO dehydrogenase that catalyzes the oxidation of CO to CO2
physiological function
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the enzyme catalyzes the oxidation of CO to CO2, thereby providing carbon and energy to the organism and maintaining subtoxic levels of CO in the troposphere
physiological function
the enzyme is a molybdenum-containing iron-sulfur flavoprotein and is the key enzyme in the chemolithoautotrophic utilization of CO by Oligotropha carboxidovorans strain OM5. Conserved protein building blocks constitute CODH and the other molybdenum hydroxylases
physiological function
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the heterodinucleating ligand LH2, i.e. (E)-3-(((2,7-di-tert-butyl-9,9-dimethyl-5-((pyridin-2-ylmethylene)amino)-9H-xanthen-4-yl)amino)methyl)benzene-1,2-diol functions as functional model of the bimetallic active site found in Mo-Cu carbon monoxide dehydrogenase. Treatment of LH2 with either Cu(I) or M(VI) (M = Mo, W) sources leads to the site-selective incorporation of the respective metals. The incorporation of both Mo(VI) and Cu(I) into L forms a highly reactive heterobimetallic complex [MoVIO3CuI(L)](NEt4)2, that triggers oxidation reactivity, in which a nucleophilic Mo(VI) trioxo attacks Cu(I)-bound imine. The major product of the reaction is a molybdenum(VI) complex [Mo(L')O2](NEt4) coordinated by a modified ligand L' that contains a new C-O bond in place of the imine functionality
physiological function
Afipia carboxidovorans ATCC 49405
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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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physiological function
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the enzyme is a molybdenum-containing iron-sulfur flavoprotein and is the key enzyme in the chemolithoautotrophic utilization of CO by Oligotropha carboxidovorans strain OM5. Conserved protein building blocks constitute CODH and the other molybdenum hydroxylases
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mechanism of Mo/Cu carbon monoxide dehydrogenase, electronic structure contributions to reactivity, overview
additional information
mechanism of Mo/Cu carbon monoxide dehydrogenase, electronic structure contributions to reactivity, overview
additional information
structure analysis and architecture of enzyme synthesized at high (Moplus CODH) and low intracellular molybdenum content (Mominus CODH), both sources are structurally very much conserved and show the same overall fold, architecture and arrangements of the molybdopterin-cytosine-dinucleotide-type of molybdenum cofactor, the type I and type II [2Fe-2S] clusters and the flavinadenine dinucleotide. The different side-chain conformations of the active-site residues S-selanyl-Cys385 and Glu757 in Moplus and Mominus CODH indicate a side-chain flexibility and a function of the Mo ion in the proper orientation of both residues. The structure of the catalytically inactive Mominus CODH indicates that an intracellular Mo-deficiency affects exclusively the active site of the enzyme as an incomplete non-functional molybdenum cofactor is synthesized. The 5'-CDP residue is present in Mominus CODH, whereas the Mo-pyranopterin moiety is absent. In Moplus CODH the selenium faces the Mo ion and flips away from the Mo site in Mominus CODH. Active site structure, overview
additional information
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the enzyme has a unique heterobimetallic Mo/Cu active site, mass spectrometric and EPR spectra analysis, overview. Key to the catalytic mechanism of the CODH site is the electronic communication between the Mo and Cu atoms
additional information
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the enzyme is noncanonical in terms of the structure of the molybdenum center, the nature of the reaction catalyzed, the type of redox-active centers that are found, or some combination of these. The active site is located in the large subunit
additional information
the enzyme possesses a deeply buried binuclear center of CO dehydrogenase activity
additional information
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the enzyme possesses a deeply buried binuclear center of CO dehydrogenase activity
additional information
the formation of the heterotrimeric complex composed of the apoflavoprotein, the molybdoprotein, and the iron-sulfur protein involves structural changes that translate into the conversion of the apoflavoprotein from non-FAD binding to FAD binding
additional information
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the formation of the heterotrimeric complex composed of the apoflavoprotein, the molybdoprotein, and the iron-sulfur protein involves structural changes that translate into the conversion of the apoflavoprotein from non-FAD binding to FAD binding
additional information
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the formation of the heterotrimeric complex composed of the apoflavoprotein, the molybdoprotein, and the iron-sulfur protein involves structural changes that translate into the conversion of the apoflavoprotein from non-FAD binding to FAD binding
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additional information
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structure analysis and architecture of enzyme synthesized at high (Moplus CODH) and low intracellular molybdenum content (Mominus CODH), both sources are structurally very much conserved and show the same overall fold, architecture and arrangements of the molybdopterin-cytosine-dinucleotide-type of molybdenum cofactor, the type I and type II [2Fe-2S] clusters and the flavinadenine dinucleotide. The different side-chain conformations of the active-site residues S-selanyl-Cys385 and Glu757 in Moplus and Mominus CODH indicate a side-chain flexibility and a function of the Mo ion in the proper orientation of both residues. The structure of the catalytically inactive Mominus CODH indicates that an intracellular Mo-deficiency affects exclusively the active site of the enzyme as an incomplete non-functional molybdenum cofactor is synthesized. The 5'-CDP residue is present in Mominus CODH, whereas the Mo-pyranopterin moiety is absent. In Moplus CODH the selenium faces the Mo ion and flips away from the Mo site in Mominus CODH. Active site structure, overview
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