The effect of pressure on the excited-state proton transfer in the wild-type green fluorescent protein

Pavel Leiderman, Dan Huppert, S. James Remington, Laren M. Tolbert, Kyril M. Solntsev*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Ultrahigh-pressure dependence of the excited-state proton transfer (ESPT) in the wild-type green fluorescence protein (wt-GFP) in D2O was measured using steady-state and picosecond time-resolved fluorescence spectroscopies. The proton dissociation rate of the chromophore is almost insensitive to a pressure increase up to about 1.1 GPa. In contrast, the diffusion-limited geminate recombination kinetics is strongly affected by pressure, decreasing the effective dimensionality of proton diffusion as pressure increased. The GFP β-barrel structure sustains the high pressure and unfolds only at P > 1.5 GPa.

Original languageEnglish
Pages (from-to)303-306
Number of pages4
JournalChemical Physics Letters
Volume455
Issue number4-6
DOIs
StatePublished - 10 Apr 2008

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