Reverse engineering a protein: the mechanochemistry of ATP synthase
Biochimica et Biophysica Acta (BBA) - BioenergeticsPublished 1 May 2000
George Oster, Hongyun Wang
Citations201
SJR quartileQ1
SJR score1.05
SNIP0.79
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TL;DR
It is shown 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.
Abstract
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.
Keywords
Biochemistry, Genetics and Molecular Biology
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