Journal ArticleDOI
Protein Conformational Dynamics Probed by Single-Molecule Electron Transfer
Haw Yang,Haw Yang,Haw Yang,Guobin Luo,Guobin Luo,Guobin Luo,Pallop Karnchanaphanurach,Pallop Karnchanaphanurach,Pallop Karnchanaphanurach,Tai Man Louie,Tai Man Louie,Tai Man Louie,Ivan Rech,Ivan Rech,Ivan Rech,Sergio Cova,Sergio Cova,Sergio Cova,Luying Xun,Luying Xun,Luying Xun,X. Sunney Xie,X. Sunney Xie,X. Sunney Xie +23 more
TLDR
By probing the fluorescence lifetime of the single flavin on a photon-by-photon basis, the variation of flavin-tyrosine distance over time is observed, suggesting the existence of multiple interconverting conformers related to the fluctuating catalytic reactivity.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.read more
Citations
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References
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