Energy coupling to ATP synthesis by the proton-translocating ATPase

Peter C. Maloney

Research output: Contribution to journalReview articlepeer-review

63 Scopus citations


This review summarizes recent work on energy coupling to ATP synthesis by the reversible, proton-translocating ATPase of mitochondria, chloroplasts, and bacteria. In the first sections, this enzyme is distinguished from other ATP-linked ion transport systems, and progress in the biochemical analysis is discussed. There is at present a reasonably consistent idea of the overall structure of the enzyme, and one can begin to assign specific functional roles to individual subunits of the complex. The latter half of this review deals with mechanisms of energy coupling, about which there is clear divergence of opinion. An "indirect coupling" model would allow for the possibility that H+ translocation transmits energy for ATP synthesis by driving the enzyme through a sequence of conformational states, so that H+ translocated need not take part in the chemistry of ATP synthesis. By contrast, a "direct coupling" mechanism would specify that H+ translocated must participate in the chemical reaction by combining with oxygen from phosphate during the synthetic step. Such discussion is preceded by an outline of the "proton well", since this idea forms the basis of one direct coupling model. In addition, it is suggested that the idea of a proton (ion) well may be of more general significance to the analysis of ion-coupled transport, because it includes the postulate that mechanistically significant ion binding can occur within the profile of the electric field. A proton (ion) well can be derived from both kinetic and equilibrium treatments, and from mechanistic considerations in fields as distinct as biochemistry and neurophysiology. As a result, it illustrates how further advances in formulating mechanisms of energy coupling might profit by a merger of technique and perspective from areas that have as a common goal an understanding of how large proteins catalyze movements of small molecules across a membrane.

Original languageEnglish (US)
Pages (from-to)1-12
Number of pages12
JournalThe Journal of Membrane Biology
Issue number1
StatePublished - Dec 1982


  • chemiosmotic theory
  • ion-coupled transport
  • membrane potential
  • oxidative phosphorylation
  • proton well
  • proton-translocating ATPase

ASJC Scopus subject areas

  • Biophysics
  • Physiology
  • Cell Biology


Dive into the research topics of 'Energy coupling to ATP synthesis by the proton-translocating ATPase'. Together they form a unique fingerprint.

Cite this