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- W2017830973 abstract "The isolation of ATP synthase (F 0 F 1 ) ( 82 ) and F 0 ( 83 ) 34 years ago finally revealed that F 0 F 1 is a motor composed of F 0 (ion-motor, abc subunits) and F 1 (ATP-motor, α 3 β 3 γδε subunits) (Fig. 1). The single molecule videotape ( 4, 5, 65, 66 ) revealed that γε axis of F 1 rotates counterclockwise, proceeds by each 2π 3 step, and is driven by torque of 42 pN·nm ( 12 ) with nearly 100% efficiency ( 5 ) (Fig. 4). The motor is composed of a rotor (γε-F 0 -c) and a stator ( α 3 β 3 δ-F 0 -ab), and the rotor is connected to a shaft (γε). Since F 0 F 1 is driven by Δ ̄ gmH + ( 9, 10, 84 ), biophysical studies on stable TF 0 F 1 ( 1, 7 ) are essential to elucidate the mechanism. These include nanomechanics ( 4, 5 ) (Fig. 4), crystallography ( 2, 3 ) (Figs. 2 and 3), NMR ( 51, 52 ), ESR ( 56 ), synchrotron analysis ( 3, 28 ), and electrophysiology ( 10, 25 ). The K mATP value of rotation is 0.8 μ m , with the V max of 3.9 rps ( 5 ). This corresponds to the bi-site catalysis in proton transport by F 0 F 1 ( 10, 70, 84 ). X-ray crystallography of MF 1 ( 2 ) and the α 3 β 3 oligomer of TF 1 ( 3 ) (Fig. 2) together with mutation analyses revealed the role of residues in the rotation. The idea of elastic energy store is proposed in α 3 β 3 γ during the stepping time (up to a few sec) after the ATP binding. Biological studies have partially clarified the genetic and kinetic regulation of the rotation in MF 1 . Both theories ( 6, 7, 62, 64, 85 ) and the biological significance ( 17 ) of the intramolecular rotation of F 0 F 1 await further studies, especially those of F 0 and minor subunits." @default.
- W2017830973 created "2016-06-24" @default.
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- W2017830973 date "1999-01-01" @default.
- W2017830973 modified "2023-09-24" @default.
- W2017830973 title "Biophysical studies on ATP synthase" @default.
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- W2017830973 doi "https://doi.org/10.1016/s0065-227x(99)80003-3" @default.
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