A T P Synthase is the universal enzyme that synthesizes A TP, the universal fuel that powers most cellular processes. This protein is constructed from two rotary motors acting in opposition, and operating by two different physical mechanisms. The F1 motor generates a mechanical torque using the hydrolysis energy of A T P. The F o motor generates a rotary torque in the opposite direction employing a transmembrane protonmotive force. The two motors are connected by a flexible coupling, and each motor can be reversed: The F o motor can drive the F 1 motor in reverse to synthesize A T P, and the F 1 motor can drive the Fo motor in reverse to pump protons. Thus, AT P synthase exhibits two of the major energy transduction pathways employed by the cell to convert chemical energy into mechanical force. A physical analysis of the F1 and F o motors can provide a unified view of the mechanochemical principles underlying these energy transducers. The figure above displays a cross section of the F1 motor showing the rotating shaft (purple and grey) surrounded by the hexamer of alternating alpha (yellow) and beta (red and green) subunits.

Research from the laboratory of Dr. George Oster in the Department of Molecular and Cell Biology will allow you to see it in action on the web.