title: High-level QM/MM modelling predicts an arginine as the acid in the condensation reaction catalysed by citrate synthase.
abstract: High-level ab initio quantum mechanical/molecular mechanical (QM/MM) modelling of citryl-CoA formation in citrate synthase reveals that an arginine residue acts as the proton donor; this proposed new mechanism helps to explain how chemical and large scale conformational changes are coupled in this paradigmatic enzyme.
authors.affiliation: Centre for Computational Chemistry, School of Chemistry, University of Bristol, Cantocks Close, Bristol, UK.
authors.forename: Marc W
authors.initials: MW
authors.lastname: van der Kamp
authors.forename: Francesca
authors.initials: F
authors.lastname: Perruccio
authors.forename: Adrian J
authors.initials: AJ
authors.lastname: Mulholland
mesh_terms: D000143:Acids / Q000737:chemistry*; D000214:Acyl Coenzyme A / Q000737:chemistry / Q000378:metabolism; D001120:Arginine / Q000737:chemistry* / Q000378:metabolism*; D002384:Catalysis; D002950:Citrate (si)-Synthase / Q000737:chemistry* / Q000378:metabolism*; D003198:Computer Simulation; D008958:Models, Molecular; D015394:Molecular Structure
chemical_list: D000143:Acids; D000214:Acyl Coenzyme A; C029890:citryl-coenzyme A; D001120:Arginine; D002950:Citrate (si)-Synthase