title: How Fo-ATPase generates rotary torque.
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.
authors.affiliation: University of California, Berkeley 94720-3112, USA.
authors.forename: G
authors.initials: G
authors.lastname: Oster
authors.forename: H
authors.initials: H
authors.lastname: Wang
authors.forename: M
authors.initials: M
authors.lastname: Grabe
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000378:metabolism*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*; D019415:Torque; D025262:Vacuolar Proton-Translocating ATPases
chemical_list: D020409:Molecular Motor Proteins; D025262:Vacuolar Proton-Translocating ATPases; D006180:Proton-Translocating ATPases