Reversible Photoisomerization of the Isolated Green Fluorescent Protein Chromophore

Carrascosa, Eduardo, Bull, James N., Scholz, Michael S., Coughlan, Neville J.A., Olsen, Seth, Wille, Uta and Bieske, Evan J. (2018) Reversible Photoisomerization of the Isolated Green Fluorescent Protein Chromophore. Journal of Physical Chemistry Letters, 9 (10). pp. 2647-2651. ISSN 1948-7185

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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 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.

Item Type: Article
Uncontrolled Keywords: materials science(all) ,/dk/atira/pure/subjectarea/asjc/2500
Faculty \ School: Faculty of Science > School of Chemistry
Related URLs:
Depositing User: LivePure Connector
Date Deposited: 28 Feb 2019 16:30
Last Modified: 02 Sep 2019 15:35
URI: https://ueaeprints.uea.ac.uk/id/eprint/70056
DOI: 10.1021/acs.jpclett.8b01201

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