Notes on the mechanism of ATP synthesis

M. A. Bianchet, Peter L. Pedersen, L. Mario Amzel

Research output: Contribution to journalShort surveypeer-review

Abstract

The most commonly quoted mechanism of the coupling between the electrochemical proton gradient and the formation of ATP from ADP and Pi assumes that all states of the F1 portion of the ATP synthase have β subunits in "tight," "loose," and "open" conformations. Models based on this assumption are inconsistent with some of the available experimental evidence. A mechanism that includes an additional β subunit conformation, "closed," observed in the rat liver structure overcomes these difficulties.

Original languageEnglish (US)
Pages (from-to)517-521
Number of pages5
JournalJournal of Bioenergetics and Biomembranes
Volume32
Issue number5
DOIs
StatePublished - 2000

Keywords

  • ATP synthesis
  • Conformational changes
  • F-ATPase

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

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