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Philosophical Transactions of the Royal Society B: Biological Sciences logoLink to Philosophical Transactions of the Royal Society B: Biological Sciences
. 2000 Apr 29;355(1396):523–528. doi: 10.1098/rstb.2000.0593

How Fo-ATPase generates rotary torque.

G Oster 1, H Wang 1, M Grabe 1
PMCID: PMC1692753  PMID: 10836505

Abstract

The F-ATPases synthesize ATP using a transmembrane ionmotive force (IMF) established by the electron transport chain. This transduction involves first converting the IMF to a rotary torque in the transmembrane Fo portion. This torque is communicated from Fo to the F1 portion where the energy is used to release the newly synthesized ATP from the catalytic sites according to Boyer's binding change mechanism. Here we explain the principle by which an IMF generates this rotary torque in the Fo ion engine.

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Selected References

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