Catalytic mechanism of F1-ATPase

Joachim Weber, Alan E. Senior

Research output: Contribution to journalReview articlepeer-review

392 Scopus citations


The structure of the core catalytic unit of ATP synthase, α3β3γ, has been determined by X-ray crystallography, revealing a roughly symmetrical arrangement of alternating α and β subunits around a central cavity in which helical portions of γ are found. A low-resolution structural model of F0, based on electron spectroscopic imaging, locates subunit a and the two copies of subunit b outside of a subunit c oligomer. The structures of individual subunits ε and c (largely) have been solved by NMR spectroscopy, but the oligomeric structure of c is still unknown. The structures of subunits a and δ remain undefined, that of b has not yet been defined but biochemical evidence indicates a credible model. Subunits γ, ε, b, and δ are at the interface between F1 and F0; γε complex forms one element of the stalk, interacting with c at the base and α and β at the top. The locations of b and δ are less clear. Elucidation of the structure F0, of the stalk, and of the entire F1F0 remains a challenging goal.

Original languageEnglish
Pages (from-to)19-58
Number of pages40
JournalBiochimica et Biophysica Acta - Bioenergetics
Issue number1
StatePublished - Mar 28 1997


  • ATP synthase, FF
  • Catalytic mechanism
  • Oxidative phosphorylation


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