The role of nickel in acetyl-CoA synthesis by the bifunctional enzyme CO dehydrogenase/acetyl-CoA synthase: enzymology and model chemistry |
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Authors: | S. W. Ragsdale Charles G. Riordan |
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Affiliation: | (1) Department of Biochemistry, Beadle Center, University of Nebraska, Lincoln, NE 68588-0622, USA, US;(2) Department of Chemistry, Kansas State University, Manhattan, KS 66506-3701, USA, US |
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Abstract: | CO dehydrogenase/acetyl-CoA synthase (CODH/ACS) is one of the four known nickel enzymes. It is a bifunctional protein that catalyzes the oxidation of CO to CO2 at a nickel iron-sulfur cluster (Cluster C) and a remarkable condensation reaction between a methyl group (donated from a methylated corrinoid iron-sulfur protein), carbon monoxide, and coenzyme A to form acetyl-CoA at a separate nickel iron-sulfur cluster (Cluster A). This review focuses on the current understanding of the structure and function of Cluster A and on related model chemistry. It describes studies that uncovered the first example of a biological organometallic reaction sequence. The mechanism of acetyl-CoA synthesis includes enzymebound methylnickel, iron-carbonyl, and acylmetal intermediates. Discovery of the methylnickel species constituted the first example of an alkylnickel species in biology and unveiled a new biological role for nickel. Received: 10 April 1996 / Accepted: 4 July 1996 |
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Keywords: | Acetyl-CoA synthesis Carbon monoxide Nickel enzymes Iron-sulfur CO dehydrogenase |
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