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Information on EC 1.2.5.3 - aerobic carbon monoxide dehydrogenase
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1.2.5.3 aerobic carbon monoxide dehydrogenaseIUBMB Comments
This enzyme, found in carboxydotrophic bacteria, catalyses the oxidation of CO to CO2 under aerobic conditions. The enzyme contains a binuclear Mo-Cu cluster in which the copper is ligated to a molybdopterin center via a sulfur bridge. The enzyme also contains two [2Fe-2S] clusters and FAD, and belongs to the xanthine oxidoreductase family. The CO2 that is produced is assimilated by the Calvin-Benson-Basham cycle, while the electrons are transferred to a quinone via the FAD site, and continue through the electron transfer chain to a dioxygen terminal acceptor . cf. EC 1.2.7.4, anaerobic carbon monoxide dehydrogenase.
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The enzyme appears in viruses and cellular organisms
Synonyms
mo-cu carbon monoxide dehydrogenase, mocu-codh, aerobic carbon monoxide dehydrogenase, molybdoenzyme carbon monoxide dehydrogenase, molybdenum-containing carbon monoxide dehydrogenase, molybdenum- and copper-dependent co dehydrogenase, molybdenum-containing co dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Carbon monoxide dehydrogenase
CO dehydrogenase
CODH
CoxS
coxSML
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EC 1.2.2.4
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formerly
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EC 1.2.3.10
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formerly
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Mo-CODH
Mo-Cu carbon monoxide dehydrogenase
Mo/Cu CODH
MoCu-CODH
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molybdenum- and copper-containing carbon monoxide dehydrogenase
molybdenum- and copper-dependent CO dehydrogenase
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molybdenum-containing carbon monoxide dehydrogenase
molybdenum/copper-containing carbon monoxide dehydrogenase
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molybdoenzyme carbon monoxide dehydrogenase
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molybdenum- and copper-containing carbon monoxide dehydrogenase
Afipia carboxidovorans ATCC 49405
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molybdenum-containing carbon monoxide dehydrogenase
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molybdenum-containing carbon monoxide dehydrogenase
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molybdenum-containing carbon monoxide dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CO + a quinone + H2O = CO2 + a quinol
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CO + a quinone + H2O = CO2 + a quinol
CO initially binds rapidly to the enzyme, possibly at the Cu(I) of the active site, prior to undergoing oxidation. A Mo(V) species exhibits strong coupling to the copper of the active center, the rate-limiting step of overall turnover is likely in the reductive half-reaction
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CO + a quinone + H2O = CO2 + a quinol
hypothetical reaction mechanism, overview
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
CO + a quinone + H2O = CO2 + a quinol
reaction mechanism that initially involves nucleophilic attack of a Mo=O oxo on the carbon center of Cu(I)-CO, resulting in a 5-membered cyclic m2-e(2) CO2-bridged Mo(VI)-Cu(I)-Cys complex I that can bind HO-/H2O to yield 1-OH. This is followed by a second nucleophilic attack on the activated mu2-nu2 CO2 carbon centre of 1-OH to yield a Mo(IV)-bicarbonate product complex, 1-P. This second nucleophilic attack is suggested based on electronic structure description of cyclic m2-e(2) CO2-bridged Mo(VI)-Cu(I)-Cys complex I, which possesses a bent and activated CO2 bound to the Mo and Cu ions. Proposed catalytic cycle for CODH that avoids formation of a stable C-S bonded cyclic m2-e(2) CO2-bridged Mo(VI)-Cu(I)-Cys complex II
CO + a quinone + H2O = CO2 + a quinol
reaction mechanism that initially involves nucleophilic attack of a Mo=O oxo on the carbon center of Cu(I)-CO, resulting in a 5-membered cyclic m2-e(2) CO2-bridged Mo(VI)-Cu(I)-Cys complex I that can bind HO-/H2O to yield 1-OH. This is followed by a second nucleophilic attack on the activated mu2-nu2 CO2 carbon centre of 1-OH to yield a Mo(IV)-bicarbonate product complex, 1-P. This second nucleophilic attack is suggested based on our electronic structure description of cyclic m2-e(2) CO2-bridged Mo(VI)-Cu(I)-Cys complex I, which possesses a bent and activated CO2 bound to the Mo and Cu ions. Proposed catalytic cycle for CODH that avoids formation of a stable C-S bonded cyclic m2-e(2) CO2-bridged Mo(VI)-Cu(I)-Cys complex II
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
carbon-monoxide:quinone oxidoreductase
This enzyme, found in carboxydotrophic bacteria, catalyses the oxidation of CO to CO2 under aerobic conditions. The enzyme contains a binuclear Mo-Cu cluster in which the copper is ligated to a molybdopterin center via a sulfur bridge. The enzyme also contains two [2Fe-2S] clusters and FAD, and belongs to the xanthine oxidoreductase family. The CO2 that is produced is assimilated by the Calvin-Benson-Basham cycle, while the electrons are transferred to a quinone via the FAD site, and continue through the electron transfer chain to a dioxygen terminal acceptor [5]. cf. EC 1.2.7.4, anaerobic carbon monoxide dehydrogenase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
CO2 + 1,2-naphthoquinol-4-sulfonic acid
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?
CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
CO2 + 1,2-naphthoquinol-4-sulfonic acid
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?
CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
CO2 + 1,2-naphthoquinol-4-sulfonic acid
Afipia carboxidovorans ATCC 49405
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?
CO + 1,4-naphthoquinone + H2O
CO2 + 1,4-naphthoquinol
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?
CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
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?
CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
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?
CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
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?
CO + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride + H2O
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
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?
CO + a quinone + H2O
CO2 + a quinol
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?
CO + a quinone + H2O
CO2 + a quinol
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the enzyme catalyzes the oxidation of CO to CO2, yielding two electrons and two H+
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?
CO + a quinone + H2O
CO2 + a quinol
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?
CO + benzoquinone + H2O
CO2 + benzoquinol
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?
CO + methyl viologen + H2O
CO2 + reduced methylene blue
methyl viologen as an electron acceptor and saturated carbon monoxide as an electron donor
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?
CO + methyl viologen + H2O
CO2 + reduced methylene blue
methyl viologen as an electron acceptor and saturated carbon monoxide as an electron donor
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?
CO + methylene blue + H2O
CO2 + NAD+
methyl blue as an electron acceptor and saturated carbon monoxide as an electron donor
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?
CO + methylene blue + H2O
CO2 + NAD+
methyl blue as an electron acceptor and saturated carbon monoxide as an electron donor
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CO + NADPH + H+ + H2O
CO2 + reduced methyl viologen
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CO + NADPH + H+ + H2O
CO2 + reduced methyl viologen
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?
CO + ubiquinone + H2O
CO2 + ubiquinol
ubiquinone is the likely physiological oxidant for CO dehydrogenase
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?
CO + ubiquinone + H2O
CO2 + ubiquinol
oxidation of carbon monoxide occurs at the binuclear center with reducing equivalents passed from the redox-active molybdenum to the proximal Fe-S cluster I to the distal Fe-S cluster II and finally to the FAD cofactor
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additional information
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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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additional information
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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
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additional information
?
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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
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?
additional information
?
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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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additional information
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analysis of mechanism of H2 oxidation, which involves initial binding of H2 to the copper of the binuclear center, displacing the bound water, followed by sequential deprotonation through a copper-hydride intermediate to reduce the binuclear center.The enzyme can be reduced by H2 with a limiting rate constant of 5.3/s and a dissociation constant Kd of 0.525 mM, steady-state and stopped-flow rapid reaction kinetics, overview
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additional information
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analysis of mechanism of H2 oxidation, which involves initial binding of H2 to the copper of the binuclear center, displacing the bound water, followed by sequential deprotonation through a copper-hydride intermediate to reduce the binuclear center.The enzyme can be reduced by H2 with a limiting rate constant of 5.3/s and a dissociation constant Kd of 0.525 mM, steady-state and stopped-flow rapid reaction kinetics, overview
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?
additional information
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quinones are unusual physiological oxidants for this family of enzymes
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?
additional information
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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
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?
additional information
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is able to catalyze both the oxidation of CO to CO2 and the oxidation of H2 to protons and electrons
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additional information
?
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is able to catalyze both the oxidation of CO to CO2 and the oxidation of H2 to protons and electrons
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additional information
?
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Afipia carboxidovorans ATCC 49405
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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?
additional information
?
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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
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?
additional information
?
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is able to catalyze both the oxidation of CO to CO2 and the oxidation of H2 to protons and electrons
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CO + a quinone + H2O
CO2 + a quinol
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?
CO + ubiquinone + H2O
CO2 + ubiquinol
ubiquinone is the likely physiological oxidant for CO dehydrogenase
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
molybdenum-containing cofactor
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the active site molybdenum center located in teh large subunit. The molybdenum becomes reduced in the final step of the reaction
seleno-molybdenum-cofactor
analysis of the architecture and arrangements of the molybdopterin-cytosine dinucleotide-type of the molybdenum cofactor. The hydrogen bonding interaction pattern of the molybdenum cofactor involves 27 hydrogen bonds with the surrounding protein. Of these, eight are with the cytosine moiety, eight with the diphosphate, six with the pyranopterin, and five with the ligands of the Mo. A 5'-CDP residue is present in Mominus CODH, whereas the Mo-pyranopterin moiety is absent. 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. Function of the Mo ion in the proper orientation of active-site residues S-selanyl-Cys385 and Glu757. Mo is an absolute requirement for the conversion of molybdopterin to MCD, a tricyclic tetra-hydropterin-pyran system reduced by two electrons when compared to the fully oxidized state, as well as for insertion of the Mo cofactor into CODH
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[2Fe-2S]-center
presence of 2 [Fe2S2] clusters, UV-vis spectrum shows a shoulder at 550 nm
[CuSMoO2] cluster
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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
FAD
FAD is bound in a fold formed by the N-terminal and middle domains. In the N-terminal domain a beta-turn part of a betaalphabeta-unit of a three-stranded parallel beta-sheet contains the motif 32AGGHS36 which interacts with the FAD diphosphate. FAD binding structure, overview
FAD
FAD is bound in the medium subunit, a flavoprotein
FAD
FAD is bound in the medium subunit. The flavoprotein can be removed from CO dehydrogenase by dissociation with sodium dodecylsulfate, the resulting M(LS)2- or (LS)2-structured CO dehydrogenase species can be reconstituted with the recombinant apoflavoprotein produced in Escherichia coli, structural and functional analysis of FAD binding in CO dehydrogenase
FAD
one noncovalently bound FAD molecule per monomer, FAD-binding occurs on the M subunit and requires conformational changes of subunit M introduced through the binding of subunt M to subunits LS. In air-oxidized CO dehydrogenase, the flavin is fully oxidized
FAD
the GLGTYG sequence, residues 564 to 569, in large subunit CoxL is identical to dinucleotide-binding motif GXGXXG/A, an FAD binding site. The FAD-binding domain of the ferredoxin-NADP+ reductase type is absent
molybdenum cofactor
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molybdopterin cytosine dinucleotide as the organic portion of the Bradyrhizobium japonicum CODH molybdenum cofactor
molybdenum cofactor
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presence of a square pyramidal (Mo) oxidized active site, i.e. [(MCD)MoVIOX(Fe-S)CuI(S-Cys)]n, MCD = molybdopterin cytosine dinucleotide, X = OH3 or O4, cofactor reaction mechanism, computational modelling, overview
molybdopterin cofactor
the L subunit carries the molybdenum cofactor, which is a mononuclear complex of Mo and molybdopterin-cytosine dinucleotide (MCD). The latter occurs in a redox state that is reduced by two electrons compared with the fully oxidized state, a tricyclic tetrahydropterin-pyran system. The MCD-molybdenum cofactor is buried at the center of the L subunit and is ligated through a dense network of hydrogen bonds originating from both domains of subunit L. The geometry of the first coordination sphere around the Mo ion is a distorted square pyramid
molybdopterin cofactor
the molybdoprotein of CO dehydrogenase carries the molybdopterin cytosine dinucleotide (MCD)1-type of molybdenum cofactor and the unique active-site loop Gly383-Val-Ala-Tyr-Arg-Cys-Ser-Phe-Arg391, which positions the catalytically essential S-selanylcysteine 388 in a distance of 3.7 A to the molybdenum ion
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
quinone
quinone cofactors interact with CODH at its FAD site
additional information
a seleno-molybdo-iron-sulfur-flavoprotein
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additional information
an S-selanylcysteine-containing 88.7-kDa molybdoprotein, a 17.8-kDa iron-sulfur protein, and a 30.2-kDa flavoprotein in a (LMS)2 subunit structure
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additional information
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an S-selanylcysteine-containing 88.7-kDa molybdoprotein, a 17.8-kDa iron-sulfur protein, and a 30.2-kDa flavoprotein in a (LMS)2 subunit structure
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additional information
CODH shows carbon monoxide oxidation activity with all tested electron acceptors, including methyl viologen, NAD+, NADP+, and methylene blue. Specific activity is increased by about 20% when NAD+ and NADP+ are used as electron acceptors, compared with methyl viologen, and by about 50% when methylene blue is used
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additional information
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presence of FAD, Fe/S clusters, and a [CuSMoO2] coordination in the active site determined by Raman spectra
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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
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additional information
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the enzyme contains 2.29 mol of Mo, 7.96 mol of Fe, 7.60 mol of S, and 1.99 mol of flavins at a 1.15:4:3.82:1 molar ratio, but contains no tungsten
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additional information
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the enzyme is a molybdo iron-sulfur flavoprotein
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additional information
the enzyme is a molybdo iron-sulfur flavoprotein containing S-selanylcysteine. The redox components of one LMS-structured monomer are the MCD-molybdenum cofactor, composed of a molybdenum ion with two oxo- and one hydroxoligand, complexed by the enedithiolene group of MCD, [2Fe-2S] clusters of type I and type II, and a noncovalently bound FAD molecule
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Cu
Fe-S cluster
proximal Fe-S cluster I and distal Fe-S cluster II
Fe2+
iron-sulfur center
two [2Fe-2S] clusters in the small subunit
Mo
Molybdenum
Se
selenium
[2Fe-2S] cluster
[CuSMoO2] cluster
additional information
Fe2+
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the small subunit CoxS harbors two [2Fe-2S] iron-sulfur clusters
Mo
the pentacoordinated Mo(VI) exhibits a distorted square pyramidal coordination geometry. Function of the Mo ion in the proper orientation of active-site residues S-selanyl-Cys385 and Glu757. Mo is an absolute requirement for the conversion of molybdopterin to MCD, a tricyclic tetra-hydropterin-pyran system reduced by two electrons when compared to the fully oxidized state, as well as for the insertion of the Mocofactor into CODH
Molybdenum
in air-oxidized CO dehydrogenase, the oxidation state of Mo is +VI
Molybdenum
Mo/Cu-containing enzyme active site. The overall configuration of the binuclear center is L-MoVIO2-microS-CuI-Cys388, with L representing a bidentate pyranopterin cofactor common to all molybdenum enzymes other than nitrogenase
selenium
an S-selanylcysteine-containing large subunit
selenium
necessity of S-selanylcysteine for the catalyzed reaction, the selenium atom of S-selanylcysteine at the active site is located in a distance of 3.7 A from the Mo ion. It is near the equatorial oxo and hydroxo group of the Mo ion
[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
[2Fe-2S] cluster
the type II 2Fe:2S center is identified in the N-terminal domain and the type I center in the C-terminal domain of the iron-sulfur protein
[2Fe-2S] cluster
two distinct [2Fe-2S] clusters, the small subunit CoxS contains motifs indicative of type I and II [2Fe-2S] cluster, structure and binding strutcures, overview
[2Fe-2S] cluster
two types of [2Fe-2S] clusters, [2Fe-2S] clusters of type I and type II, the two [2Fe-2S] clusters are located in the S subunit. These prosthetic groups form a pathway for the electrons to the FAD. The C-terminal domain (residues 77-161) carries the proximal [2Fe-2S] cluster. The cluster is buried in CO dehydrogenase about 11 A below the protein surface at the interface between the S and the L subunit and is adjacent to the MCD-molybdenum cofactor. The [2Fe-2S] cluster is located at the N terminus of two alpha-helices that participate in a four-helix bundle of twofold symmetry
[2Fe-2S] cluster
two [2Fe-2S] iron-sulfur clusters in the small subunit
[CuSMoO2] cluster
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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
[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
additional information
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metal contents are determined by inductively coupled plasma atomic emission spectrometry
additional information
the binuclear active site contains copper as well as molybdenum
additional information
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the binuclear active site contains copper as well as molybdenum
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
additional information
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the enzyme contains 2.29 mol of Mo, 7.96 mol of Fe, 7.60 mol of S, and 1.99 mol of flavins at a 1.15:4:3.82:1 molar ratio, but contains no tungsten
additional information
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iodoacetamide
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yields di(carboxamidomethyl)molybdopterin cytosine dinucleotide from reaction with the molybdenum cofactor
additional information
thiol inhibition of CO dehydrogenase
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
rapid reaction kinetics, steady-state kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
51.1
CO
-
pH 7.2, 25°C, reductive half-reaction of enzyme CODH with CO
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.96
purified native enzyme, pH 8.0, 95°C, using 1 mM methyl blue as electron acceptor
2.1
purified native enzyme, pH 8.0, 95°C, using 1 mM methyl viologen as electron acceptor
2.45
purified native enzyme, pH 8.0, 95°C, using 1 mM NADP+ as electron acceptor
2.47
purified ative enzyme, pH 8.0, 95°C, using 1 mM NAD+ as electron acceptor
2.6
recombinant purified enzyme, reconstitution of the active site with sulfur and copper, pH 7.2, 30°C