Journal article

Reversible Photoisomerization of the Isolated Green Fluorescent Protein Chromophore

E Carrascosa, JN Bull, MS Scholz, NJA Coughlan, S Olsen, U Wille, EJ Bieske

Journal of Physical Chemistry Letters | AMER CHEMICAL SOC | Published : 2018

Abstract

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 phot..

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University of Melbourne Researchers