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Issue 31, 2015
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How far can a single hydrogen bond tune the spectral properties of the GFP chromophore?

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Abstract

Photoabsorption of the hydrogen-bonded complex of a neutral and an anionic Green Fluorescent Protein chromophore has been studied using a new dual-detection approach to action-absorption spectroscopy. Following absorption of one photon, dissociation through a single channel ensures that the full absorption spectrum is measured. Our theoretical account of the spectral shape reveals that the anionic 0–0 transition (464 nm) is blue-shifted compared to that of the wild-type protein (478 nm) due to the stronger H-bond in the dimer, and represents an upper bound for that of the isolated anion. At the same time, the apparent effect of the H-bond for the neutral chromophore is as large as 0.5 eV, red-shifting the absorption maximum of the isolated neutral (340 nm) to that measured in the dimer (393 nm) and various proteins (∼395 nm). This shift results from changes in the topography of potential-energy surfaces in the Franck–Condon region of the H-bonded systems.

Graphical abstract: How far can a single hydrogen bond tune the spectral properties of the GFP chromophore?

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Supplementary files

Article information


Submitted
13 May 2015
Accepted
18 Jun 2015
First published
23 Jun 2015

Phys. Chem. Chem. Phys., 2015,17, 20056-20060
Article type
Communication
Author version available

How far can a single hydrogen bond tune the spectral properties of the GFP chromophore?

H. V. Kiefer, E. Lattouf, N. W. Persen, A. V. Bochenkova and L. H. Andersen, Phys. Chem. Chem. Phys., 2015, 17, 20056
DOI: 10.1039/C5CP02764K

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