Journal of Bioenergetics and Biomembranes

, Volume 37, Issue 6, pp 441–444 | Cite as

Zooming in on ATP Hydrolysis in F1

  • Markus Dittrich
  • Klaus Schulten


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.

Key Words

F1-ATPase ATP hydrolysis QM/MM molecular mechanics 


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Copyright information

© Springer Science + Business Media, Inc. 2005

Authors and Affiliations

  1. 1.Beckman InstituteUniversity of Illinois at Urbana–ChampaignUrbana

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