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Science 10 October 2003:
Vol. 302. no. 5643, pp. 262 - 266
DOI: 10.1126/science.1086911
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Reports

Protein Conformational Dynamics Probed by Single-Molecule Electron Transfer

Haw Yang,1* Guobin Luo,1 Pallop Karnchanaphanurach,1 Tai-Man Louie,2 Ivan Rech,3 Sergio Cova,3 Luying Xun,2 X. Sunney Xie1{dagger}

Electron transfer is used as a probe for angstrom-scale structural changes in single protein molecules. In a flavin reductase, the fluorescence of flavin is quenched by a nearby tyrosine residue by means of photo-induced electron transfer. By probing the fluorescence lifetime of the single flavin on a photon-by-photon basis, we were able to observe the variation of flavin-tyrosine distance over time. We could then determine the potential of mean force between the flavin and the tyrosine, and a correlation analysis revealed conformational fluctuation at multiple time scales spanning from hundreds of microseconds to seconds. This phenomenon suggests the existence of multiple interconverting conformers related to the fluctuating catalytic reactivity.

1 Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
2 School of Molecular Biosciences, Washington State University, Pullman, WA 99164, USA.
3 Department of Electronics and Information, Politecnico di Milano and Centro Elettronica Quantistica e Strumentazione Elettronica Council of National Research, 20133 Milano, Italy.



* Present address: Department of Chemistry, University of California, Berkeley, CA 94720, USA.

{dagger} To whom correspondence should be addressed. E-mail: xie{at}chemistry.harvard.edu

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