Crystallographic evidence for a CO/CO2 tunnel gating mechanism in the bifunctional carbon monoxide dehydrogenase/acetyl coenzyme A synthase from Moorella thermoacetica
- 24 June 2004
- journal article
- review article
- Published by Springer Nature in JBIC Journal of Biological Inorganic Chemistry
- Vol. 9 (5) , 525-532
- https://doi.org/10.1007/s00775-004-0565-9
Abstract
Acetyl coenzyme A synthase (ACS) acts in concert with carbon monoxide dehydrogenase (CODH) to catalyze the formation of acetyl-coenzyme A from CO2-derived CO and CH3 + molecules. Recent crystal structures have shown that the three globular domains constituting the ACS subunit may be arranged in either a closed or an open conformation. A long hydrophobic tunnel network allows diffusion of CO between the CODH and the ACS active sites in the closed form, but it is blocked in the open form. On the other hand, the active site of ACS is only accessible for coenzyme A and the methyl donating protein in the open domain conformation. Although several metal compositions have been observed for this active site, present consensus is that it consists of a Ni-Ni-[Fe4S4] cluster. The observed conformational changes of ACS and the resulting different substrate accessibilities of the catalytic central nickel are reviewed here in the context of a putative CO2/CO tunnel gating mechanism.Keywords
This publication has 49 references indexed in Scilit:
- X-ray Magnetic Circular Dichroism of Pseudomonas aeruginosa Nickel(II) AzurinJournal of the American Chemical Society, 2004
- Chemically Distinct Ni Sites in the A-Cluster in Subunit β of the Acetyl-CoA Decarbonylase/Synthase Complex from Methanosarcina thermophila: Ni L-Edge Absorption and X-ray Magnetic Circular Dichroism AnalysesJournal of the American Chemical Society, 2003
- The A-Cluster in Subunit β of the Acetyl-CoA Decarbonylase/Synthase Complex from Methanosarcina thermophila: Ni and Fe K-Edge XANES and EXAFS AnalysesJournal of the American Chemical Society, 2003
- Computational Studies on the A Cluster of Acetyl-Coenzyme A Synthase: Geometric and Electronic Properties of the NiFeC Species and Mechanistic ImplicationsJournal of the American Chemical Society, 2003
- Carbon Monoxide Dehydrogenase from Clostridium thermoaceticum: Quaternary Structure, Stoichiometry of Its SDS-Induced Dissociation, and Characterization of the Faster-Migrating FormBiochemistry, 1996
- Influence of Sulfur Metalation on the Accessibility of the NiII/I Couple in [N,N‘-Bis(2-mercaptoethyl)-1,5-diazacyclooctanato]nickel(II): Insight into the Redox Properties of [NiFe]-HydrogenaseInorganic Chemistry, 1996
- Assembly of an Exchange-Coupled [Ni:Fe4S4] Cluster in the α Metallosubunit of Carbon Monoxide Dehydrogenase fromClostridium thermoaceticumwith Spectroscopic Properties and CO-Binding Ability Mimicking Those of the Acetyl-CoA Synthase Active SiteJournal of the American Chemical Society, 1996
- Reactivity of a Paramagnetic Enzyme−CO Adduct in Acetyl-CoA Synthesis and CleavageBiochemistry, 1996
- Substrate and Accessory Protein Requirements and Thermodynamics of Acetyl-CoA Synthesis and Cleavage in Methanosarcina barkeriBiochemistry, 1995
- Redox titrations of carbon monoxide dehydrogenase from Clostridium thermoaceticumBiochemistry, 1992