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.
Original language | English |
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Pages (from-to) | 2647-2651 |
Number of pages | 5 |
Journal | Journal of Physical Chemistry Letters |
Volume | 9 |
Issue number | 10 |
Early online date | 3 May 2018 |
DOIs | |
Publication status | Published - 17 May 2018 |
Profiles
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James Bull
- School of Chemistry, Pharmacy and Pharmacology - Associate Professor in Ultrafast Chemical Physics
- Centre for Photonics and Quantum Science - Member
- Chemistry of Light and Energy - Member
Person: Research Group Member, Academic, Teaching & Research