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Significance F1 -ATPase is a small motor protein, composed of 3 α- and 3 β-subunits that surround a central γ-subunit. The β-subunits alternate cyclically between 2 major conformational states to produce the rotation of the γ-subunit. Although the rotation on the microsecond timescale is powered by the differential binding of ATP and its hydrolysis products ADP and HPO4 2− , there is near-100% conversion efficiency of the free energy of ATP hydrolysis, which occurs on the picosecond timescale. The free-energy profile constructed for the 360° rotation cycle shows that F1 -ATPase achieves its high energy-conversion efficiency by elegantly separating fast catalytic events, which involve small local conformational changes, from the slow binding/release of ligands involved in the large conformational change.

Insights into the origin of the high energy-conversion efficiency of F 1 -ATPase

Insights into the origin of the high energy-conversion efficiency of F ₁ -ATPase