36 degree step size of proton-driven c-ring rotation in FoF1-ATP synthase
| dc.creator | Dueser, Monika G. | |
| dc.creator | Zarrabi, Nawid | |
| dc.creator | Cipriano, Daniel J. | |
| dc.creator | Ernst, Stefan | |
| dc.creator | Glick, Gary D. | |
| dc.creator | Dunn, Stanley D. | |
| dc.creator | Boersch, Michael | |
| dc.date | 2009-03-01 | |
| dc.date.accessioned | 2026-06-02T21:44:31Z | |
| dc.description | Synthesis of the biological "energy currency molecule" adenosine triphosphate ATP is accomplished by FoF1-ATP synthase. In the plasma membrane of Escherichia coli, proton-driven rotation of a ring of 10 c subunits in the Fo motor powers catalysis in the F1 motor. While F1 uses 120 degree stepping, Fo models predict a step-by-step rotation of c subunits 36 degree at a time, which is here demonstrated by single-molecule fluorescence resonance energy transfer. | |
| dc.description | 8 pages, 1 figure | |
| dc.identifier | https://arxiv.org/abs/0903.0184 | |
| dc.identifier | http://arxiv.org/abs/0903.0184 | |
| dc.identifier.uri | https://demo.dspace.org/handle/10673/2156 | |
| dc.subject | Biomolecules | |
| dc.subject | Quantitative Methods | |
| dc.title | 36 degree step size of proton-driven c-ring rotation in FoF1-ATP synthase | |
| dc.type | text |