Regensburg 2004 – wissenschaftliches Programm
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SYLS: Life Sciences on the Nanometer Scale - Physics Meets Biology
SYLS 3: Symposium "Life Sciences on the Nanometer Scale - Physics Meets Biology"
SYLS 3.44: Poster
Mittwoch, 10. März 2004, 16:00–18:30, B
Single-molecule microscopy of the rotary motor F0F1 ATP synthase at work — •Michael Prummer1, Horst Vogel1, Beate Sick2, Alois Renn3, Gert Zumofen3, Urs P. Wild3, Georg Kaim4, and Peter Dimroth4 — 1Institute of Biomolecular Sciences, EPFL, CH-1015 Lausanne — 2DNA-Array Facility, University of Lausanne, CH-1015 Lausanne — 3Physical Chemistry Laboratory, ETH-Hönggerberg, CH-8093 Zürich — 4Institute of Microbiology, ETH-Zentrum, CH-8092 Zürich
The universal ATP factory F0F1 ATP synthase is the smallest rotary motor in nature. The driving force for rotation during ATP production is a trans-membrane potential together with a H+/Na+ gradient. Vice versa, F0F1 can act as an ion pump by consuming ATP and is thus a completely reversible rotor. We have investigated the rotation of individual immobilized and functionally coupled F0F1 rotary motors during ATP synthesis and hydrolysis by single-fluorophore multi-parameter confocal microscopy. Simultaneously, a number of parameters have been recorded, like the emission polarization, the fluorescence lifetime, the anisotropy decay time, and the spectral relaxation time. These fluorescence quantities can be correlated with structural and functional features of the protein being part of the nano-environment of the fluorophore.