Mechanism of the F(1)F(0)-type ATP synthase, a biological rotary motor

Trends Biochem Sci. 2002 Mar;27(3):154-60. doi: 10.1016/s0968-0004(01)02051-5.


The F(1)F(0)-type ATP synthase is a key enzyme in cellular energy interconversion. During ATP synthesis, this large protein complex uses a proton gradient and the associated membrane potential to synthesize ATP. It can also reverse and hydrolyze ATP to generate a proton gradient. The structure of this enzyme in different functional forms is now being rapidly elucidated. The emerging consensus is that the enzyme is constructed as two rotary motors, one in the F(1) part that links catalytic site events with movements of an internal rotor, and the other in the F(0) part, linking proton translocation to movements of this F(0) rotor. Although both motors can work separately, they must be connected together to interconvert energy. Evidence for the function of the rotary motor, from structural, genetic and biophysical studies, is reviewed here, and some uncertainties and remaining mysteries of the enzyme mechanism are also discussed.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Adenosine Triphosphate / metabolism*
  • Bacteria / enzymology
  • Membrane Potentials
  • Models, Molecular
  • Molecular Motor Proteins
  • Protein Conformation
  • Protein Folding
  • Proton-Translocating ATPases / chemistry
  • Proton-Translocating ATPases / physiology*
  • Rotation


  • Molecular Motor Proteins
  • Adenosine Triphosphate
  • Proton-Translocating ATPases