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Proceedings Paper

Asymmetry of rotational catalysis of single membrane-bound F0F1-ATP synthase
Author(s): Nawid Zarrabi; Boris Zimmermann; Manuel Diez; Peter Graeber; Joerg Wrachtrup; Michael Boersch
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Paper Abstract

Synthesis of the cellular 'energy currency' ATP is catalyzed by membrane-bound F0F1-ATP synthases. The chemical reaction at three binding sites in the F1 part is coupled to proton translocation through the membrane-integrated F0 part by an internal rotation of subunits. We examined the rotary movements of the ε-subunit of the 'rotor' with respect to the b-subunits of the 'stator' by single-molecule fluorescence resonance energy transfer (FRET). Rotation of ε during ATP hydrolysis is divided into three major steps with constant FRET level corresponding to three binding sites. Different catalytic activities of the individual binding sites were observed depending on the relative orientation of the 'rotor'. Computer simulations of the FRET signals and non-equally distributed orientations of ε strongly corroborate asymmetry of catalysis in F0F1-ATP synthase.

Paper Details

Date Published: 29 March 2005
PDF: 14 pages
Proc. SPIE 5699, Imaging, Manipulation, and Analysis of Biomolecules and Cells: Fundamentals and Applications III, (29 March 2005); doi: 10.1117/12.597967
Show Author Affiliations
Nawid Zarrabi, Univ. Stuttgart (Germany)
Boris Zimmermann, Albert-Ludwigs-Univ. Freiburg (Germany)
Manuel Diez, Albert-Ludwigs-Univ. Freiburg (Germany)
Peter Graeber, Albert-Ludwigs-Univ. Freiburg (Germany)
Joerg Wrachtrup, Univ. Stuttgart (Germany)
Michael Boersch, Univ. Stuttgart (Germany)


Published in SPIE Proceedings Vol. 5699:
Imaging, Manipulation, and Analysis of Biomolecules and Cells: Fundamentals and Applications III
Dan V. Nicolau; Ramesh Raghavachari; Dan V. Nicolau; Jörg Enderlein; Robert C. Leif; Daniel L. Farkas, Editor(s)

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