Journal
NATURE COMMUNICATIONS
Volume 4, Issue -, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/ncomms2460
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Funding
- European Research Council [208650]
- EPSRC [EP/I003304/1]
- National Science Foundation [CHE-1026369]
- Engineering and Physical Sciences Research Council [EP/I003304/1] Funding Source: researchfish
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1026369] Funding Source: National Science Foundation
- EPSRC [EP/I003304/1] Funding Source: UKRI
- European Research Council (ERC) [208650] Funding Source: European Research Council (ERC)
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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
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