Origin of the nonexponential dynamics of excited-state proton transfer in wt-green fluorescent protein

R. Gepshtein; P. Leiderman; Dan Huppert

doi:10.1021/jp711372s

Origin of the nonexponential dynamics of excited-state proton transfer in wt-green fluorescent protein

R. Gepshtein, P. Leiderman, Dan Huppert^*

^*Corresponding author for this work

School of Chemistry

Tel Aviv University

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

We used an inhomogeneous excited-state proton-transfer kinetics model to explain the origin of the non-exponential time-resolved emission of the A-band of wt-green fluorescence protein. The calculated fit is rather good for both H₂O and D₂O samples in a wide temperature range of 80-229 K. We attribute the inhomogeneous kinetics to the distance dependence of the excited-state proton-transfer rate between the proton donor (the hydroxyl group of the chromophore) and the oxygen of a nearby water molecule.

Original language	English
Pages (from-to)	7203-7210
Number of pages	8
Journal	Journal of Physical Chemistry B
Volume	112
Issue number	24
DOIs	https://doi.org/10.1021/jp711372s
State	Published - 19 Jun 2008

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abstract = "We used an inhomogeneous excited-state proton-transfer kinetics model to explain the origin of the non-exponential time-resolved emission of the A-band of wt-green fluorescence protein. The calculated fit is rather good for both H2O and D2O samples in a wide temperature range of 80-229 K. We attribute the inhomogeneous kinetics to the distance dependence of the excited-state proton-transfer rate between the proton donor (the hydroxyl group of the chromophore) and the oxygen of a nearby water molecule.",

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AU - Leiderman, P.

AU - Huppert, Dan

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N2 - We used an inhomogeneous excited-state proton-transfer kinetics model to explain the origin of the non-exponential time-resolved emission of the A-band of wt-green fluorescence protein. The calculated fit is rather good for both H2O and D2O samples in a wide temperature range of 80-229 K. We attribute the inhomogeneous kinetics to the distance dependence of the excited-state proton-transfer rate between the proton donor (the hydroxyl group of the chromophore) and the oxygen of a nearby water molecule.

AB - We used an inhomogeneous excited-state proton-transfer kinetics model to explain the origin of the non-exponential time-resolved emission of the A-band of wt-green fluorescence protein. The calculated fit is rather good for both H2O and D2O samples in a wide temperature range of 80-229 K. We attribute the inhomogeneous kinetics to the distance dependence of the excited-state proton-transfer rate between the proton donor (the hydroxyl group of the chromophore) and the oxygen of a nearby water molecule.

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JO - Journal of Physical Chemistry B

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Origin of the nonexponential dynamics of excited-state proton transfer in wt-green fluorescent protein

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