Chemo-mechanical coupling in the rotary molecular motor f1-atpase

Abstract

F1-ATPase is a molecular motor in which the central γ subunit rotates inside the cylinder made of α3β3 subunits. The rotation is powered by ATP hydrolysis in three catalytic sites, and reverse rotation of the γ subunit by an external force leads to ATP synthesis in the catalytic sites. Single-molecule studies have revealed how the mechanical rotation is coupled to the chemical reactions in the three catalytic sites: binding/release of ATP, ADP, and phosphate, and hydrolysis/synthesis of ATP.