Spectroscopic and computational insights into the geometric and electronic properties of the A-cluster of acetyl-coenzyme A synthase.
For the last two decades, the bifunctional enzyme acetyl-coenzyme A synthase/carbon monoxide dehydrogenase (ACS/CODH) from Moorella thermoacetica has been the subject of considerable research aimed at elucidating the geometric and electronic properties of the A-cluster, which serves as the active site for ACS catalysis. While the recent success in obtaining high-resolution X-ray structures of this enzyme solved many of the mysteries regarding the number, identities, and coordination environments of the metal centers of the A-cluster, fundamental questions concerning the catalytic mechanism of this highly elaborate polynuclear active site have yet to be answered. This Commentary summarizes relevant information obtained from spectroscopic and computational studies on the oxidized, reduced, and CO-bound forms of the A-cluster and highlights some of the key issues regarding the electronic properties and reactivity of this cluster that need to be addressed in future studies.
Brunold
Thomas C
TC
Department of Chemistry, University of Wisconsin, Madison, WI 53706, USA. brunold@chem.wisc.edu
D000106:Acetate-CoA Ligase / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D003013:Clostridium / Q000201:enzymology; D019295:Computational Biology; D018360:Crystallography, X-Ray; D004583:Electrons; D008670:Metals / Q000737:chemistry / Q000378:metabolism; D008968:Molecular Conformation; D009097:Multienzyme Complexes / Q000737:chemistry / Q000378:metabolism; D013053:Spectrophotometry
D008670:Metals; D009097:Multienzyme Complexes; D000106:Acetate-CoA Ligase