Literature summary for 1.2.5.3 extracted from

Wilcoxen, J.; Hille, R.
The hydrogenase activity of the molybdenum/copper-containing carbon monoxide dehydrogenase of Oligotropha carboxidovorans (2013), J. Biol. Chem., 288, 36052-36060.

Search for more literature for 1.2.5.3

Metals/Ions

Metals/Ions	Comment	Organism	Structure
copper	Mo/Cu-containing enzyme active site	Afipia carboxidovorans
Fe-S cluster	proximal Fe-S cluster I and distal Fe-S cluster II	Afipia carboxidovorans
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	Afipia carboxidovorans
additional information	the binuclear active site contains copper as well as molybdenum	Afipia carboxidovorans

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
CO + ubiquinone + H2O	Afipia carboxidovorans	-	CO2 + ubiquinol	-	?

Organism

Organism	UniProt	Comment	Textmining
Afipia carboxidovorans	P19919 and P19920 and P19921	genes coxL, coxM, and coxS; genes coxS, coxM, and coxL	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
CO + ubiquinone + H2O	-	Afipia carboxidovorans	CO2 + ubiquinol	-	?
CO + ubiquinone + H2O	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	Afipia carboxidovorans	CO2 + ubiquinol	-	?
additional information	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	Afipia carboxidovorans	?	-	?

Subunits

Subunits	Comment	Organism
heterohexamer	(alphabetagamma)2 hexamer, with a large subunit (coxL, 88.7 kDa) containing the binuclear active site, a medium subunit (coxM, 30.2 kDa) with FAD, and a small subunit (coxS, 30.2 kDa) containing two spinach ferredoxin-like [2Fe-2S] clusters	Afipia carboxidovorans

Synonyms

Synonyms	Comment	Organism
CO dehydrogenase	-	Afipia carboxidovorans
molybdenum/copper-containing carbon monoxide dehydrogenase	-	Afipia carboxidovorans

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Afipia carboxidovorans

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.2	-	assay at	Afipia carboxidovorans

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Afipia carboxidovorans
Mo/Cu cofactor	-	Afipia carboxidovorans
ubiquinone	-	Afipia carboxidovorans

General Information

General Information	Comment	Organism
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	Afipia carboxidovorans

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Release 2023.1 (January 2023)