Molecular mechanism and energetics of coupling between substrate binding and product release in the F₁-ATPase catalytic cycle.

ABSTRACT: F₁-ATPase is a motor protein that couples the rotation of its rotary [Formula: see text] subunit with ATP synthesis or hydrolysis. Single-molecule experiments indicate that nucleotide binding and release events occur almost simultaneously during the synthesis cycle, allowing the energy gain due to spontaneous binding of ADP to one catalytic [Formula: see text] subunit to be directly harnessed for driving the release of ATP from another rather than being dissipated as heat. Here, we examine the unknown mechanism of this coupling that is critical for an exceptionally high mechanochemical efficiency of F₁-ATPase by means of all-atom free-energy simulations. We find that nondissipative and kinetically fast progression of the motor in the synthesis direction requires a con

SUBMITTER: Badocha M 

PROVIDER: S-EPMC9974484 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature