
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 F o portion. This torque is communicated from F o to the F 1 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 F o ion engine.
Models, Molecular, Proton-Translocating ATPases, Vacuolar Proton-Translocating ATPases, Torque, Protein Conformation, Molecular Motor Proteins, Molecular Sequence Data, Animals, Amino Acid Sequence
Models, Molecular, Proton-Translocating ATPases, Vacuolar Proton-Translocating ATPases, Torque, Protein Conformation, Molecular Motor Proteins, Molecular Sequence Data, Animals, Amino Acid Sequence
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