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A Ni-Fe-Cu Center in a Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase

Tzanko I. Doukov, Tina M. Iverson, Javier Seravalli, Stephen W. Ragsdale and Catherine L. Drennan
Science
New Series, Vol. 298, No. 5593 (Oct. 18, 2002), pp. 567-572
Stable URL: http://www.jstor.org/stable/3832587
Page Count: 6
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A Ni-Fe-Cu Center in a Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase
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Abstract

A metallocofactor containing iron, sulfur, copper, and nickel has been discovered in the enzyme carbon monoxide dehydrogenase/acetyl-CoA (coenzyme A) synthase from Moorella thermoacetica (f. Clostridium thermoaceticum). Our structure at 2.2 angstrom resolution reveals that the cofactor responsible for the assembly of acetyl-CoA contains a $[Fe_{4}S_{4}]$ cubane bridged to a copper-nickel binuclear site. The presence of these three metals together in one cluster was unanticipated and suggests a newly discovered role for copper in biology. The different active sites of this bifunctional enzyme complex are connected via a channel, 138 angstroms long, that provides a conduit for carbon monoxide generated at the C-cluster on one subunit to be incorporated into acetyl-CoA at the A-cluster on the other subunit.

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