Protein conformational dynamics probed by single-molecule electron transfer

Haw Yang, Guobin Luo, Pallop Karnchanaphanurach, Tai Man Louie, Ivan Rech, Sergio Cova, Luying Xun, X. Sunney Xie

Research output: Contribution to journalArticle

701 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)262-266
Number of pages5
JournalScience
Volume302
Issue number5643
DOIs
StatePublished - Oct 10 2003
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General

Fingerprint Dive into the research topics of 'Protein conformational dynamics probed by single-molecule electron transfer'. Together they form a unique fingerprint.

  • Cite this

    Yang, H., Luo, G., Karnchanaphanurach, P., Louie, T. M., Rech, I., Cova, S., Xun, L., & Xie, X. S. (2003). Protein conformational dynamics probed by single-molecule electron transfer. Science, 302(5643), 262-266. https://doi.org/10.1126/science.1086911