Zooming in on ATP hydrolysis in F1

Markus Dittrich, Klaus Schulten

Research output: Contribution to journalReview articlepeer-review


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 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.

Original languageEnglish (US)
Pages (from-to)441-444
Number of pages4
JournalJournal of Bioenergetics and Biomembranes
Issue number6
StatePublished - Dec 2005
Externally publishedYes


  • ATP
  • F1-ATPase
  • Hydrolysis
  • Molecular mechanics
  • QM/MM

ASJC Scopus subject areas

  • Physiology
  • Cell Biology


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