Chemomechanical coupling of F(1)-ATPase under hydrolysis conditions

F(1)-ATPase (F(1)) is the smallest rotary motor protein that couples ATP hydrolysis/synthesis to rotary motion in a highly reversible manner. F(1) is unique compared with other motor proteins because of its high efficiency and reversibility in converting chemical energy into mechanical work. To determine the energy conversion mechanism of F(1)-ATPase, we developed a novel single-molecule manipulation technique with magnetic tweezers and determined the timing of P(i) release, which was the last unknown piece of the chemomechanical coupling scheme of F(1). The established fundamental chemomechanical coupling scheme provides evidence to explain the high reversibility between catalysis and mechanical work.