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Updated: Aug 8, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
Zooming in on ATP hydrolysis in F1
Markus Dittrich1, Klaus Schulten
1Beckman Institute, University of Illinois at Urbana-Champaign, 405 N, Mathews Avenue, Urbana, Illinois 61801, USA. kschulte@ks.uiuc.edu
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.
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