Unraveling the Structure and Mechanism of Acetyl-Coenzyme A Synthase

The bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A (CoA) synthase (CODH/ACS) is a key enzyme in the Wood−Ljungdahl pathway of carbon fixation. Carbon monoxide is combined with a methyl group and ultimately converted to acetyl-CoA at a unique Ni-containing bimetallic site in the...

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Bibliographic Details
Published in:Accounts of chemical research 2004-10, Vol.37 (10), p.775-783
Main Author: Hegg, Eric L
Format: Article
Language:English
Subjects:
Acetate-CoA Ligase - chemistry
Acetate-CoA Ligase - metabolism
Models, Molecular
Molecular Structure
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Summary:The bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A (CoA) synthase (CODH/ACS) is a key enzyme in the Wood−Ljungdahl pathway of carbon fixation. Carbon monoxide is combined with a methyl group and ultimately converted to acetyl-CoA at a unique Ni-containing bimetallic site in the A-cluster of this enzyme. Despite years of extensive biochemical and spectroscopic studies and the recent report of three separate crystal structures, the mechanism by which acetyl-CoA is synthesized is still unknown. Over the past two years there have been a number of significant developments regarding ACS. This Account critically examines these recent developments and especially focuses on those areas that are still a matter of debate.
ISSN:0001-4842
1520-4898
DOI:10.1021/ar040002e