The binding of a proton to one of the c-subunits in the (*) F0 produces a 1/10 turn in the gamma subunit of this protein, in turn driving a conformational change in the alpha-beta subunit which allows for the binding of the namesake molecule.
One theory about how these structures evolved posits that they originally were used by the cell to break down the compound they now synthesize. Its action was observed in an experiment in which a fluorescent filament of actin was attached to its gamma subunit and turned counterclockwise in the presence of a certain molecule. The F0 complex of this protein forms a channel through the membrane, whereas the F1 complex stretches into the matrix. The binding of a proton to one of the c-subunits in the (*) F0 produces a 1/10 turn in the gamma subunit of this protein, in turn driving a conformational change in the alpha-beta subunit which allows for the binding of the namesake molecule. FTP, name this enzyme present in the mitochondrion, which creates a highly energetic molecule via phosphorylation.
One theory about how these structures evolved posits that they originally were used by the cell to break down the compound they now synthesize.
{ATP synthase} ({also} accept {ATP synthetase}, {Adenosine Tri}-{Phosphate synthase}, etc.)