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Journal Article

Dramatic modulation of electron transfer in protein complexes by crosslinking

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons78394

Messerschmidt,  A.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

van Amsterdam, I. M. C., Ubbink, M., Einsle, O., Messerschmidt, A., Merli, A., Cavazzini, D., et al. (2002). Dramatic modulation of electron transfer in protein complexes by crosslinking. Nature Structural Biology, 9(1), 48-52.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6FFE-0
Abstract
The transfer of electrons between proteins is an essential step in biological energy production. Two protein redox partners are often artificially crosslinked to investigate the poorly understood mechanism by which they interact. To better understand the effect of crosslinking on electron transfer rates, we have constructed dimers of azurin by crosslinking the monomers. The measured electron exchange rates, combined with crystal structures of the dimers, demonstrate that the length of the linker can have a dramatic effect on the structure of the dimer and the electron transfer rate. The presence of ordered water molecules in the protein protein interface may considerably influence the electronic coupling between redox centers.