Notes on the mechanism of ATP synthesis

J Bioenerg Biomembr. 2000 Oct;32(5):517-21. doi: 10.1023/a:1005673209883.

Abstract

The most commonly quoted mechanism of the coupling between the electrochemical proton gradient and the formation of ATP from ADP and P(i) assumes that all states of the F(1) portion of the ATP synthase have beta 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 beta subunit conformation, "closed," observed in the rat liver structure overcomes these difficulties.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Adenosine Triphosphate / biosynthesis*
  • Animals
  • Catalytic Domain
  • Electrochemistry
  • Mitochondria, Liver / enzymology
  • Mitochondrial Proton-Translocating ATPases / chemistry
  • Mitochondrial Proton-Translocating ATPases / metabolism
  • Models, Biological
  • Models, Molecular
  • Protein Conformation
  • Protein Structure, Quaternary
  • Protein Subunits
  • Proton-Translocating ATPases / chemistry
  • Proton-Translocating ATPases / metabolism*
  • Rats

Substances

  • Protein Subunits
  • Adenosine Triphosphate
  • Mitochondrial Proton-Translocating ATPases
  • Proton-Translocating ATPases