The rotary binding change mechanism of ATP synthases

AbstractThe F0F1 ATP synthase functions as a rotary motor where subunit rotation driven by a current of protons flowing through F0 drives the binding changes in F1 that are required for net ATP synthesis. Recent work that has led to the identification of components of the rotor and stator is reviewed. In addition, a model is proposed to describe the transmission of energy from four proton transport steps to the synthesis of one ATP. Finally, some of the requirements for efficient energy coupling by a rotary binding change mechanism are considered