Reversible photoisomerization of the isolated green fluorescent protein chromophore

Eduardo Carrascosa, James N. Bull, Michael S. Scholz, Neville J. A. Coughlan, Seth Olsen, Uta Wille, Evan J. Bieske

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24 Citations (Scopus)


Fluorescent proteins have revolutionized the visualization of biological processes, prompting efforts to understand and control their intrinsic photophysics. Here we investigate the photoisomerization of deprotonated p-hydroxybenzylidene-2,3-dimethylimidazolinone anion (HBDI-), the chromophore in green fluorescent protein and in Dronpa protein, where it plays a role in switching between fluorescent and nonfluorescent states. In the present work, isolated HBDI- molecules are switched between the Z and E forms in the gas phase in a tandem ion mobility mass spectrometer outfitted for selecting the initial and final isomers. Excitation of the S1 ← S0 transition provokes both Z → E and E → Z photoisomerization, with a maximum response for both processes at 480 nm. Photodetachment is a minor channel at low light intensity. At higher light intensities, absorption of several photons in the drift region drives photofragmentation, through channels involving CH3 loss and concerted CO and CH3CN loss, although isomerization remains the dominant process.

Original languageEnglish
Pages (from-to)2647-2651
Number of pages5
JournalJournal of Physical Chemistry Letters
Issue number10
Early online date3 May 2018
Publication statusPublished - 17 May 2018

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