Rotational coupling in the F0F1 ATP synthase

Robert K. Nakamoto, Christian J. Ketchum, Marwan K. Al-Shawi

Research output: Contribution to journalArticle

Abstract

The F0F1 ATP synthase is a large multisubunit complex that couples translocation of protons down an electrochemical gradient to the synthesis of ATP. Recent advances in structural analyses have led to the demonstration that the enzyme utilizes a rotational catalytic mechanism. Kinetic and biochemical evidence is consistent with the expected equal participation of the three catalytic sites in the α3β3 hexamer, which operate in sequential, cooperative reaction pathways. The rotation of the core γ subunit plays critical roles in establishing the conformation of the sites and the cooperative interactions. Mutational analyses have shown that the rotor subunits are responsible for coupling and in doing so transmit specific conformational information between transport and catalysis.

Original languageEnglish (US)
Pages (from-to)205-234
Number of pages30
JournalAnnual Review of Biophysics and Biomolecular Structure
Volume28
DOIs
StatePublished - 1999
Externally publishedYes

Keywords

  • Active transport
  • ATPase
  • Catalytic cooperativity
  • Proton transport
  • Subunit interactions

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology

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