Excited-State Dynamics in the Green Fluorescent Protein Chromophore

The remarkable suppression of radiationless decay by the green fluorescent protein (GFP) is investigated through ultrafast fluorescence spectroscopy of its isolated chromophore in solution. Decay data are measured by fluorescence up-conversion as a function of solvent and wavelength for both neutral...

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Bibliographic Details
Published in:The journal of physical chemistry. B 2004-01, Vol.108 (3), p.1102-1108
Main Authors: Mandal, Debabrata, Tahara, Tahei, Meech, Stephen R
Format: Article
Language:English
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Summary:The remarkable suppression of radiationless decay by the green fluorescent protein (GFP) is investigated through ultrafast fluorescence spectroscopy of its isolated chromophore in solution. Decay data are measured by fluorescence up-conversion as a function of solvent and wavelength for both neutral and anionic forms of the chromophore. All fluorescence decays are found to be well described by two exponentially decaying components. The effect of medium viscosity is slight, suggesting that the intramolecular motion promoting radiationless decay is a volume-conserving one. A minor effect of solvent polarity and H-bonding ability on the decay times is observed. The two decay constants are independent of emission wavelength, but their relative weights are not. Time-resolved fluorescence spectroscopy shows that the Stokes shift is complete in
ISSN:1520-6106
1520-5207
DOI:10.1021/jp035816b