Ground-state proton transfer in the photoswitching reactions of the fluorescent protein Dronpa

Mark M. Warren, Marius Kaucikas, Ann Fitzpatrick, Paul Champion, J. Timothy Sage and Jasper J. van Thor ()
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Mark M. Warren: Imperial College London, South Kensington Campus, London SW7 2AZ, UK
Marius Kaucikas: Imperial College London, South Kensington Campus, London SW7 2AZ, UK
Ann Fitzpatrick: Imperial College London, South Kensington Campus, London SW7 2AZ, UK
Paul Champion: Northeastern University
J. Timothy Sage: Northeastern University
Jasper J. van Thor: Imperial College London, South Kensington Campus, London SW7 2AZ, UK

Nature Communications, 2013, vol. 4, issue 1, 1-8

Abstract: Abstract The reversible photoswitching between the ‘on’ and ‘off’ states of the fluorescent protein Dronpa involves photoisomerization as well as protein side-chain rearrangements, but the process of interconversion remains poorly characterized. Here we use time-resolved infrared measurements to monitor the sequence of these structural changes, but also of proton transfer events, which are crucial to the development of spectroscopic contrast. Light-induced deprotonation of the chromophore phenolic oxygen in the off state is a thermal ground-state process, which follows ultrafast (9 ps) trans–cis photoisomerization, and so does not involve excited-state proton transfer. Steady-state infrared difference measurements exclude protonation of the imidazolinone nitrogen in both the on and off states. Pump–probe infrared measurements of the on state reveal a weakening of the hydrogen bonding between Arg66 and the chromophore C=O, which could be central to initiating structural rearrangement of Arg66 and His193 coinciding with the low quantum yield cis–trans photoisomerization

Date: 2013
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DOI: 10.1038/ncomms2460

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