Abstract
• A single molecule of F 1-ATPase is by itself a rotary motor in which a central subunit, γ, rotates against a surrounding stator cylinder made of α 3β 3 hexamer. • Driven by the three β subunits that hydrolyse ATP sequentially, the motor runs with discrete 120° steps at low ATP concentrations. • Over broad ranges of load and speed, the motor produces a constant torque of 40 pN·nm. • The mechanical work the motor does in the 120° step, or the work per ATP hydrolysed, is also constant and amounts to 80-90 pN·nm, which is close to the free energy of ATP hydrolysis. Thus this motor can work at near 100% efficiency.
Original language | English |
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Pages (from-to) | 3-18 |
Number of pages | 16 |
Journal | Essays in Biochemistry |
Volume | 35 |
Publication status | Published - 2000 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry