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