PMID:18048691

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Citation

Jeoung, JH and Dobbek, H (2007) Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon monoxide dehydrogenase. Science 318:1461-4

Abstract

Anaerobic 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.

Links

PubMed Online version:10.1126/science.1148481

Keywords

Aldehyde Oxidoreductases/chemistry; Aldehyde Oxidoreductases/isolation & purification; Aldehyde Oxidoreductases/metabolism; Anaerobiosis; Binding Sites; Carbon Dioxide/metabolism; Carbon Monoxide/metabolism; Crystallization; Crystallography, X-Ray; Iron/chemistry; Iron/metabolism; Ligands; Multienzyme Complexes/chemistry; Multienzyme Complexes/isolation & purification; Multienzyme Complexes/metabolism; Nickel/chemistry; Nickel/metabolism; Peptococcaceae/enzymology; Protein Conformation; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism

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