Dipole-bound states in the meta form of the green fluorescent protein chromophore observed by cryogenic action spectroscopy

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Authors: Anne P. Rasmussen, Nikolaj Klinkby, Lars H. Andersen
Cited by: 0
References: 57

Abstract

. Complementary DFT (ωB97X-D/aug-cc-pVTZ) calculations provide insight into the structure and vibrational resonances of the excess electron in this biologically relevant chromophore. The results extend the understanding of dipole-bound and resonance states in complex molecular systems. We find that one low-energy mode of the neutral radical is particularly Franck-Condon active. The same mode has previously been found to dominate absorption spectra of other GFP-chromophore derivatives. It is suggested that the DRSs are potential doorway states for capture of low energy electrons.

Fields of Study & Subjects

Spectroscopy and Quantum Chemical Studies Atomic and Molecular Physics Advanced Chemical Physics Studies

Publication details

Journal / source
Physical Chemistry Chemical Physics
Volume
28
Issue
5
Pages
3168–3173
Publication date
1 January 2026
Language
EN