Issue 2, 2017

ortho and para chromophores of green fluorescent protein: controlling electron emission and internal conversion

Abstract

Green fluorescent protein (GFP) continues to play an important role in the biological and biochemical sciences as an efficient fluorescent probe and is also known to undergo light-induced redox transformations. Here, we employ photoelectron spectroscopy and quantum chemistry calculations to investigate how the phenoxide moiety controls the competition between electron emission and internal conversion in the isolated GFP chromophore anion, following photoexcitation with ultraviolet light in the range 400–230 nm. We find that moving the phenoxide group from the para position to the ortho position enhances internal conversion back to the ground electronic state but that adding an additional OH group to the para chromophore, at the ortho position, impedes internal conversion. Guided by quantum chemistry calculations, we interpret these observations in terms of torsions around the C–C–C bridge being enhanced by electrostatic repulsions or impeded by the formation of a hydrogen-bonded seven-membered ring. We also find that moving the phenoxide group from the para position to the ortho position reduces the energy required for detachment processes, whereas adding an additional OH group to the para chromophore at the ortho position increases the energy required for detachment processes. These results have potential applications in tuning light-induced redox processes of this biologically and technologically important fluorescent protein.

Graphical abstract: ortho and para chromophores of green fluorescent protein: controlling electron emission and internal conversion

Supplementary files

Article information

Article type
Edge Article
Submitted
26 8月 2016
Accepted
05 11月 2016
First published
07 11月 2016
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY license

Chem. Sci., 2017,8, 1621-1630

ortho and para chromophores of green fluorescent protein: controlling electron emission and internal conversion

C. McLaughlin, M. Assmann, M. A. Parkes, J. L. Woodhouse, R. Lewin, H. C. Hailes, G. A. Worth and H. H. Fielding, Chem. Sci., 2017, 8, 1621 DOI: 10.1039/C6SC03833F

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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