3b52
From Proteopedia
Ni,Fe-CODH-600 mV state + CO2
Structural highlights
Function[COOS2_CARHZ] CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH) (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAnaerobic CO dehydrogenases catalyze the reversible oxidation of CO to CO2 at a complex Ni-, Fe-, and S-containing metal center called cluster C. We report crystal structures of CO dehydrogenase II from Carboxydothermus hydrogenoformans in three different states. In a reduced state, exogenous CO2 supplied in solution is bound and reductively activated by cluster C. In the intermediate structure, CO2 acts as a bridging ligand between Ni and the asymmetrically coordinated Fe, where it completes the square-planar coordination of the Ni ion. It replaces a water/hydroxo ligand bound to the Fe ion in the other two states. The structures define the mechanism of CO oxidation and CO2 reduction at the Ni-Fe site of cluster C. Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon monoxide dehydrogenase.,Jeoung JH, Dobbek H Science. 2007 Nov 30;318(5855):1461-4. PMID:18048691[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Carhz | Large Structures | Dobbek, H | Jeoung, J H | 4fe-4 | Cluster c | Cytoplasm | Iron | Iron-sulfur | Membrane | Metal-binding | Nickel | Oxidoreductase
