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A set formed by five reversibly-switchable fluorescent proteins (RSFPs)display spread over 40~nm in absorption maxima and only 18~nm in emission. Thefive proteins -- Dronpa, rsFastLime, rsKame, Padron(anionic form) and bsDronpa-- carry exactly the same chromophore and differ just in a few mutations. Thusthey form an ideal set for mechanistic investigation. Starting with the resultsof molecular dynamics simulations we use QM/MM calculations to investigate theeffects controlling the spectral tuning . In this contribution we show that themodels, which are based on CASPT2//CASSCF level of QM theory, reproduce theobserved absorption trend with only a limited blue-shift of 4.5 kcal/mol andemission trend with even smaller blue-shift of 1.5 kcal/mol. Using CASSCF QM/MMcalculations we analyze the chromophore's charge-transfer patterns during theabsorption and emission, which, in turn trigger a cascade ofhydrogen-bond-network rearrangements indicating a preparation to anisomerization event. We also show how the contribution of individual aminoacidsto the chromophore conformational changes correlates with spectral tuning ofthe absorption and emission. Furthermore, we identify how the conicalintersection topography correlates with protein's photophysical properties. Inconclusion, we establish a detailed mechanistic explanation of variations inphoto-switching speed as well as higher sensitivity of RSFPs to mutationobserved for light absorption relative to light emission.

On excited state reaction path in reversibly switchable fluorescent proteins