Probing the Microsolvation Environment of the Green Fluorescent Protein Chromophore In Vacuo

Zagorec-Marks, Wyatt; Foreman, Madison M.; Verlet, Jan R.R.; Weber, J. Mathias

doi:10.1021/acs.jpclett.0c00105

Probing the Microsolvation Environment of the Green Fluorescent Protein Chromophore In Vacuo

Zagorec-Marks, Wyatt; Foreman, Madison M.; Verlet, Jan R.R.; Weber, J. Mathias

Authors

Wyatt Zagorec-Marks

Madison M. Foreman

Professor Jan Verlet j.r.r.verlet@durham.ac.uk
Professor

J. Mathias Weber

Abstract

We present vibrational and electronic photodissociation spectra of a model chromophore of the green fluorescent protein in complexes with up to two water molecules, prepared in a cryogenic ion trap at 160–180 K. We find the band origin of the singly hydrated chromophore at 20 985 cm–1 (476.5 nm) and observe partially resolved vibrational signatures. While a single water molecule induces only a small shift of the S1 electronic band of the chromophore, without significant change of the Franck–Condon envelope, the spectrum of the dihydrate shows significant broadening and a greater blue shift of the band edge. Comparison of the vibrational spectra with predicted infrared spectra from density functional theory indicates that water molecules can interact with the oxygen atom on the phenolate group or on the imidazole moiety, respectively.

Citation

Zagorec-Marks, W., Foreman, M. M., Verlet, J. R., & Weber, J. M. (2020). Probing the Microsolvation Environment of the Green Fluorescent Protein Chromophore In Vacuo. Journal of Physical Chemistry Letters, 11(5), 1940-1946. https://doi.org/10.1021/acs.jpclett.0c00105

Journal Article Type	Article
Acceptance Date	Feb 19, 2020
Online Publication Date	Feb 19, 2020
Publication Date	Mar 5, 2020
Deposit Date	May 13, 2020
Publicly Available Date	Feb 19, 2021
Journal	Journal of Physical Chemistry Letters
Publisher	American Chemical Society
Peer Reviewed	Peer Reviewed
Volume	11
Issue	5
Pages	1940-1946
DOI	https://doi.org/10.1021/acs.jpclett.0c00105