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Probing the Microsolvation Environment of the Green Fluorescent Protein Chromophore In Vacuo by Zagorec-Marks, Wyatt; Foreman, Madison M.; Verlet, Jan R. R.; Weber, J. Mathias is a Materials Science article available to read on EtoBox.

What is Probing the Microsolvation Environment of the Green Fluorescent Protein Chromophore In Vacuo about?

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 S 1 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.

Who reads Probing the Microsolvation Environment of the Green Fluorescent Protein Chromophore In Vacuo?

Author

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

Publisher

American Chemical Society; American Chemical Society (ACS); Publons (ISSN 1948-7185)

Published

2020

Language

EN

Field

Materials Science (Physical Sciences)