The vacuolar H+-ATPases (V-ATPases) are a universal class of proton pumps t
hat are structurally similar to the F-ATPases. Both protein families are ch
aracterized by a membrane-bound segment (V-0, F-0) responsible for the tran
slocation of protons, and a soluble portion, (V-1, F-1), which supplies the
energy for translocation by hydrolyzing ATP. Here we present a mechanochem
ical model for the functioning of the V-0 ion pump that is consistent with
the known structural features and biochemistry. The model reproduces a vari
ety of experimental measurements of performance and provides a unified view
of the many mechanisms of intracellular pH regulation.