Understanding ATP synthesis: Structure and mechanism of the F1-ATPase (Review)

Research output: Contribution to journalArticle

Abstract

To couple the energy present in the electrochemical proton gradient, established across the mitochondrial membrane by the respiratory chain, to the formation of ATP from ADP and Pi, ATP-synthase goes through a sequence of coordinated conformational changes of its major subunits (α, β). These changes are induced by the rotation of the γ subunit driven by the translocation of protons through the c subunit of the membrane portion of the enzyme. During this process, the F1-portion of the ATP-synthase adopts at least two major conformations depending on the occupancy of the β subunits: one with two nucleotides, the other with three. In the two-nucleotide structure, the empty β subunit adopts an open conformation that is highly different from the other conformations of β subunits: tight, loose and closed. The three-dimensional structures of the F1-ATPase in each of these two major conformations provide a framework for understanding the mechanism of energy coupling by the enzyme. The energetics associated with two different models of the reaction steps, analysed using molecular dynamics calculations, show that three-nucleotide intermediates do not occur in configurations with an open β subunit; instead, they are stabilized by completing a jaw-like motion that closes the β subunit around the nucleotide. Consequently, the energy driven, major conformational change takes place with the β subunits in the tight, loose and closed conformation.

Original languageEnglish (US)
Pages (from-to)27-33
Number of pages7
JournalMolecular Membrane Biology
Volume20
Issue number1
DOIs
StatePublished - Jan 2003

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Proton-Translocating ATPases
Nucleotides
Adenosine Triphosphate
Protons
Mitochondrial Membranes
Enzymes
Molecular Dynamics Simulation
Electron Transport
Jaw
Adenosine Diphosphate
Membranes

Keywords

  • ATP synthesis
  • F1-ATPase
  • Jaw-like motion
  • Rotational catalysis

ASJC Scopus subject areas

  • Cell Biology

Cite this

Understanding ATP synthesis : Structure and mechanism of the F1-ATPase (Review). / Leyva, J. Alfonso; Bianchet, Mario Antonio; Amzel, Mario L.

In: Molecular Membrane Biology, Vol. 20, No. 1, 01.2003, p. 27-33.

Research output: Contribution to journalArticle

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