Spectroscopic and computational insights into the geometric and electronic properties of the A-cluster of acetyl-coenzyme A synthase

• Published in: Journal of biological inorganic chemistry Vol. 9; no. 5; pp. 533 - 541
• Main Author: Brunold, Thomas C.
• Format: Journal Article
• Language: English
• Published: Germany 01.07.2004
• Subjects: Acetate-CoA Ligase - chemistry; Acetate-CoA Ligase - metabolism; Binding Sites; Clostridium - enzymology; Computational Biology; Crystallography, X-Ray; Electrons; Metals - chemistry; Metals - metabolism; Molecular Conformation; Multienzyme Complexes - chemistry; Multienzyme Complexes - metabolism; Spectrophotometry
• ISSN: 0949-8257; 1432-1327
• DOI: 10.1007/s00775-004-0566-8

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.