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

doi:10.1126/science.1086911

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 journal › Article › peer-review

800 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 language	English (US)
Pages (from-to)	262-266
Number of pages	5
Journal	Science
Volume	302
Issue number	5643
DOIs	https://doi.org/10.1126/science.1086911
State	Published - Oct 10 2003
Externally published	Yes

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title = "Protein conformational dynamics probed by single-molecule electron transfer",

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.",

author = "Haw Yang and Guobin Luo and Pallop Karnchanaphanurach and Louie, {Tai Man} and Ivan Rech and Sergio Cova and Luying Xun and Xie, {X. Sunney}",

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T1 - Protein conformational dynamics probed by single-molecule electron transfer

AU - Yang, Haw

AU - Luo, Guobin

AU - Karnchanaphanurach, Pallop

AU - Louie, Tai Man

AU - Rech, Ivan

AU - Cova, Sergio

AU - Xun, Luying

AU - Xie, X. Sunney

PY - 2003/10/10

Y1 - 2003/10/10

N2 - 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.

AB - 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.

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DO - 10.1126/science.1086911

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Protein conformational dynamics probed by single-molecule electron transfer

Abstract

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