title: Unraveling the structure and mechanism of acetyl-coenzyme A synthase.
abstract: 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.
authors.affiliation: Department of Chemistry, University of Utah, 315 South 1400 East, Salt Lake City, Utah 84112-0850, USA. hegg@chem.utah.edu
authors.forename: Eric L
authors.initials: EL
authors.lastname: Hegg
mesh_terms: D000106:Acetate-CoA Ligase / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D015394:Molecular Structure
chemical_list: D000106:Acetate-CoA Ligase