Regensburg 2004 – wissenschaftliches Programm
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SYLS: Life Sciences on the Nanometer Scale - Physics Meets Biology
SYLS 5: Symposium "Life Sciences on the Nanometer Scale - Physics Meets Biology"
SYLS 5.2: Vortrag
Donnerstag, 11. März 2004, 11:45–12:00, H 37
Probing individual F0F1 ATP synthases by multi-parameter fluorescence spectroscopy — •Michael Prummer1, Horst Vogel1, Beate Sick2, Alois Renn3, Gert Zumofen3, Urs P. Wild3, Georg Kaim4 und 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 rotary motor F0F1 ATP synthase is the universal ATP factory in most cells from bacteria to plants and animals. The driving force for ATP production is a trans-membrane potential plus 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 simultaneously measured several fluorescence quantities from individual immobilized and functionally coupled F0F1 rotary motors by single-fluorophore multi-parameter confocal microscopy. By analyzing these quantities we could monitor the rotation of F0F1 during ATP synthesis and hydrolysis. We could further correlate for example the different distributions of the fluorescence lifetime or the emission spectral ratio with structural and functional features of the protein.