Elastic coupling mechanism of the F
1-ATPase power stroke. (
A) Catalytic dwell (0°) after ATP hydrolysis at β
D. Tightly wound γ−coiled-coil and (αβ)
3-ring are tethered (
). Power stroke starts by β
E-Pi release to allow coiled-coil unwinding. (
B) Phase 1 rotation (0°–60°): γ−coiled-coil torsion spring unwinds to equilibrium γ-foot domain position of 34°. β
E binds ATP at any phase 1 rotational position, 34° is optimal. β
D dissociates ADP optimally at 34° but can slow phase 2 if delayed. (
C) Phase 1 → phase 2 switch at 60° when the γ−coiled-coil reaches the winding limit. Electrostatic interactions between Mg-ATP and groups on the β
E lever and catalytic domains force conformational changes to break γ−coiled-coil tether and push β
E lever against subunit γ to rotate foot and coiled-coil. A different tether (
) may cause a second spring (80°–100°). (
D) Catalytic dwell begins when γ-foot reaches 120°, and β-subunit conformations change (β
E → β
T and β
D → β
E). ATP hydrolysis rewinds torsion spring.