 Solution

ATP synthase combines a membrane $F_o$ proton-conducting rotor with an $F_1$ catalytic head. The c-ring and central gamma shaft rotate relative to a stator and the alpha/beta head. Proton flow down its electrochemical potential can drive conformational changes in three beta catalytic sites to bind substrates, form and release ATP. Reverse operation uses ATP hydrolysis to turn the shaft and pump protons. The immobilized $F_1$ assay isolates this latter rotation; it does not require the membrane proton motor to be present.