Projects per year
Abstract
The photophysics of the chromophore of the green fluorescent protein in Aequorea victoria (avGFP) are dominated by an excited state proton transfer reaction. In contrast the photophysics of the same chromophore in solution are dominated by radiationless decay, and photoacid behaviour is not observed. Here we show that modification of the pKa of the chromophore by fluorination leads to an excited state proton transfer on an extremely fast (50 fs) time scale. Such a fast rate suggests a barrierless proton transfer and the existence of a pre-formed acceptor site in the aqueous solution, which is supported by solvent and deuterium isotope effects. In addition, at lower pH, photochemical formation of the elusive zwitterion of the GFP chromophore is observed by means of an equally fast excited state proton transfer from the cation. The significance of these results for understanding and modifying the properties of fluorescent proteins are discussed
Original language | English |
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Pages (from-to) | 5747-5752 |
Number of pages | 6 |
Journal | Chemical Science |
Volume | 7 |
Issue number | 9 |
Early online date | 6 Jun 2016 |
DOIs | |
Publication status | Published - 19 Aug 2016 |
Keywords
- excited state proton transfer
- Photoacid
- GFP
- Ultrafast
Profiles
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Steve Meech
- School of Chemistry, Pharmacy and Pharmacology - Professor of Physical Chemistry
- Centre for Photonics and Quantum Science - Member
- Chemistry of Light and Energy - Member
Person: Research Group Member, Academic, Teaching & Research
Projects
- 2 Finished
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Photodynamics in second generation fluorescent proteins
Meech, S., Bulman Page, P. & Heisler, I.
Engineering and Physical Sciences Research Council
1/08/10 → 31/03/14
Project: Research