(1) Beckman Institute, University of Illinois at Urbana–Champaign, 405 N, Mathews Avenue, Urbana, Illinois, 61801
Abstract:
We summarize our current view of the reaction mechanism in F1-ATPase as it has emerged from experiment, theory, and computational studies over the last several years. ATP catalysis in the catalytic binding pockets of F1 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.
