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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Grants
Awarded by Australian Research Council
Funding Acknowledgements
We thank Professor R Jockusch and Professor L. Andersen for sharing data from refs 24 and 20, respectively. We thank the Australian Research Council for financial support under the Discovery Project Scheme (DP150101427 and DP160100474). E.C. acknowledges support by the Austrian Science Fund (FWF) through a Schrodinger Fellowship (No. J4013-N36). M.S.S. thanks the Australian government for an Australian Postgraduate Award scholarship.