title: Zooming in on ATP hydrolysis in F1.
abstract: We summarize our current view of the reaction mechanism in F(1)-ATPase as it has emerged from experiment, theory, and computational studies over the last several years. ATP catalysis in the catalytic binding pockets of F(1) takes place without the release of any significant free energy and is efficiently driven by the combined action of two water molecules utilizing a so-called protein-relay mechanism. The chemical reaction itself is controlled by the spatial position of a key arginine residue.
authors.affiliation: Beckman Institute, University of Illinois at Urbana-Champaign, 405 N, Mathews Avenue, Urbana, Illinois 61801, USA. kschulte@ks.uiuc.edu
authors.forename: Markus
authors.initials: M
authors.lastname: Dittrich
authors.forename: Klaus
authors.initials: K
authors.lastname: Schulten
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D020134:Catalytic Domain; D006868:Hydrolysis; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism; D014867:Water / Q000378:metabolism
chemical_list: D014867:Water; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases