36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase
Synthesis of adenosine triphosphate ATP, the 'biological energy currency', is accomplished by F(o)F(1)-ATP synthase. In the plasma membrane of Escherichia coli, proton-driven rotation of a ring of 10 c subunits in the F(o) motor powers catalysis in the F(1) motor. Although F(1) uses 120 de...
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| Veröffentlicht in: | The EMBO journal 2009-09, Vol.28 (18), p.2689-2696 |
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| container_title | The EMBO journal |
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| creator | Düser, Monika G Zarrabi, Nawid Cipriano, Daniel J Ernst, Stefan Glick, Gary D Dunn, Stanley D Börsch, Michael |
| description | Synthesis of adenosine triphosphate ATP, the 'biological energy currency', is accomplished by F(o)F(1)-ATP synthase. In the plasma membrane of Escherichia coli, proton-driven rotation of a ring of 10 c subunits in the F(o) motor powers catalysis in the F(1) motor. Although F(1) uses 120 degrees stepping during ATP synthesis, models of F(o) predict either an incremental rotation of c subunits in 36 degrees steps or larger step sizes comprising several fast substeps. Using single-molecule fluorescence resonance energy transfer, we provide the first experimental determination of a 36 degrees sequential stepping mode of the c-ring during ATP synthesis. |
| doi_str_mv | 10.1038/emboj.2009.213 |
| format | Article |
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| ispartof | The EMBO journal, 2009-09, Vol.28 (18), p.2689-2696 |
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| source | MEDLINE; Springer Nature OA Free Journals; Access via Wiley Online Library; EZB-FREE-00999 freely available EZB journals; Wiley Online Library (Open Access Collection); PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Adenosine Triphosphate - metabolism Biophysics - methods Catalysis Escherichia coli - enzymology Fluorescence Resonance Energy Transfer - methods Lipid Bilayers - chemistry Models, Biological Monte Carlo Method Mutation Photons Plasmids - metabolism Protein Conformation Proton-Translocating ATPases - metabolism Proton-Translocating ATPases - physiology Protons Rotation |
| title | 36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase |
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