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A Structural Perspective on Mechanism and Function of the Cytochrome bc1 Complex

MPS-Authors
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Hunte,  Carola
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Solmaz,  Sozanne R.N.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Palsdottir,  Hildur
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Wenz,  Tina
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Hunte, C., Solmaz, S. R., Palsdottir, H., & Wenz, T. (2008). A Structural Perspective on Mechanism and Function of the Cytochrome bc1 Complex. In G. Schäfer, & H. S. Penefsky (Eds.), Results and Problems in Cell Differentiation (pp. 253-278). Berlin, Heidelberg: Springer-Verlag Berlin Heidelberg 2007. doi:10.1007/400_2007_042.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-D841-B
Abstract
The cytochrome bc1 complex is a fundamental component of the energy conversion machinery of respiratory and photosynthetic electron transfer chains. The multi-subunit membrane protein complex couples electron transfer from hydroquinone to cytochrome c to the translocation of protons across the membrane, thereby substantially contributing to the proton motive force that is used for ATP synthesis. Considerable progress has been made with structural and functional studies towards complete elucidation of the Q cycle mechanism, which was originally proposed by Mitchell 30 years ago. Yet, open questions regarding key steps of the mechanism still remain. The role of the complex as a major source of reactive oxygen species and its implication in pathophysiological conditions has recently gained interest.