Nickel-containing carbon monoxide dehydrogenase/acetyl-CoA synthase
- Univ. of Nebraska, Lincoln, NE (United States). Dept. of Biochemistry
This article reviews an enzyme with two important catalytic activities, carbon monoxide dehydrogenase (CODH) (reaction 1) and acetyl-CoA synthase (ACS) (reaction 2). These reactions are key to an autotrophic pathway that has become known as the reductive acetyl-CoA or the Wood/Ljungdahl pathway. ACS also catalyzes two exchange reactions that have been valuable in elucidating the mechanism of acetyl-CoA synthesis: an exchange reaction between CO and the carbonyl group of acetyl-CoA (reaction 3) and an exchange reaction between free CoA and the CoA moiety of acetyl-CoA (reaction 4). Ten years ago, one of the authors (Ragsdale) and Harland Wood, first proposed that the CODH from acetogenic bacteria catalyzes the final steps in acetyl-CoA synthesis and, therefore, should be renamed acetyl-CoA synthase. It was previously accepted that these steps occurred on a cobalt-containing corrinoid protein. This was a controversial proposal that required the existence of carbonyl, methyl, and acetyl enzyme adducts. Proof of this postulate was nontrivial since it required the characterization of enzyme-bound intermediates. With the goal of detecting and characterizing intermediates in the pathway, the authors` laboratory and others began to probe the enzyme in the resting state and at different stages of the catalytic cycle with sensitive spectroscopic methods. This review summarizes the fruits of the combined labor of the laboratories working on this interesting problem. 237 refs.
- Sponsoring Organization:
- USDOE, Washington, DC (United States); National Insts. of Health, Bethesda, MD (United States)
- OSTI ID:
- 415589
- Journal Information:
- Chemical Reviews, Journal Name: Chemical Reviews Journal Issue: 7 Vol. 96; ISSN 0009-2665; ISSN CHREAY
- Country of Publication:
- United States
- Language:
- English
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