How does transmembrane electrochemical potential drive the rotation of Fo motor in an ATP synthase?

ABSTRACT: While the field of ATP synthase research has a long history filled with landmark discoveries, recent structural works provide us with important insights into the mechanisms that links the proton movement with the rotation of the Fo motor. Here, we propose a mechanism of unidirectional rotation of the Fo complex, which is in agreement with these new structural insights as well as our more general ΔΨ-driving hypothesis of membrane proteins: A proton path in the rotor-stator interface is formed dynamically in concert with the rotation of the Fo rotor. The trajectory of the proton viewed in the reference system of the rotor (R-path) must lag behind that of the stator (S-path). The proton moves from a higher energy site to a lower site following both trajectories simultaneously. The two traject

SUBMITTER: Zhang XC 

PROVIDER: S-EPMC4624678 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature