Reverse engineering a protein: the mechanochemistry of ATP synthase.
ATP synthase comprises two rotary motors in one. The F(1) motor can generate a mechanical torque using the hydrolysis energy of ATP. The F(o) motor generates a rotary torque in the opposite direction, but it employs a transmembrane proton motive force. Each motor can be reversed: The F(o) motor can drive the F(1) motor in reverse to synthesize ATP, and the F(1) motor can drive the F(o) motor in reverse to pump protons. Thus ATP synthase exhibits two of the major energy transduction pathways employed by the cell to convert chemical energy into mechanical force. Here we show how a physical analysis of the F(1) and F(o) motors can provide a unified view of the mechanochemical principles underlying these energy transducers.
Oster
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Department of Molecular and Cellular Biology and College of Natural Resources, University of California, Berkeley, CA 94720-3112, USA. goster@nature.berkeley.edu
Wang
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H
D000255:Adenosine Triphosphate / Q000737:chemistry; D001696:Biomechanical Phenomena; D007700:Kinetics; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry*; D011487:Protein Conformation; D015202:Protein Engineering; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D055672:Static Electricity
D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases