Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8299088 | Biochimica et Biophysica Acta (BBA) - Bioenergetics | 2008 | 4 Pages |
Abstract
The torque generated by the power stroke of Escherichia coli F1-ATPase was determined as a function of the load from measurements of the velocity of the γ-subunit obtained using a 0.25 µs time resolution and direct measurements of the drag from 45 to 91 nm gold nanorods. This result was compared to values of torque calculated using four different drag models. Although the γ-subunit was able to rotate with a 20à increase in viscosity, the transition time decreased from 0.4 ms to 5.26 ms. The torque was measured to be 63 ± 8 pN nm, independent of the load on the enzyme.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Tassilo Hornung, Robert Ishmukhametov, David Spetzler, James Martin, Wayne D. Frasch,