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Biophys J, September 2001, p. 1220-1233, Vol. 81, No. 3
Division of Biophysics, University of Osnabrück, D-49069 Osnabrück, Germany
ATP synthase (FOF1) operates as
two rotary motor/generators coupled by a common shaft. Both portions,
F1 and FO, are rotary steppers. Their
symmetries are mismatched (C3 versus C10-14). We used the curvature of fluorescent actin filaments, attached to the
rotating c-ring, as a spring balance (flexural rigidity of
8 · 10
26 Nm2) to gauge the angular
profile of the output torque at FO during ATP hydrolysis by
F1 (see theoretical companion article (Cherepanov, D. A., and W. Junge, 2001. Biophys. J. 81:1234-1244.)). The
large average output torque (50 ± 6 pN · nm) proved the
absence of any slip. Variations of the torque were small, and the
output free energy of the loaded enzyme decayed almost linearly over
the angular reaction coordinate. Considering the threefold stepping and
high activation barrier of the driving motor proper, the rather
constant output torque implied a soft elastic power transmission
between F1 and FO. It is considered as
essential, not only for the robust operation of this ubiquitous enzyme
under symmetry mismatch, but also for a high turnover rate of the two
counteracting and stepping motor/generators.
Biophys J, September 2001, p. 1220-1233, Vol. 81, No. 3
© 2001 by the Biophysical Society 0006-3495/01/09/1220/14 $2.00
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