Ultrafast action chemistry in slow motion: Atomistic description of the excitation and fluorescence processes in an archetypal fluorescent protein

Pau Armengol, Lasse Spörkel, Ricard Gelabert, Miquel Moreno, Walter Thiel, José M. Lluch

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2 Citations (Scopus)

Abstract

© 2018 the Owner Societies. We report quantum mechanical/molecular mechanical non-adiabatic molecular dynamics simulations on the electronically excited state of green fluorescent protein mutant S65T/H148D. We examine the driving force of the ultrafast (τ < 50 fs) excited-state proton transfer unleashed by absorption in the A band at 415 nm and propose an atomistic description of the two dynamical regimes experimentally observed [Stoner Ma et al., J. Am. Chem. Soc., 2008, 130, 1227]. These regimes are explained in terms of two sets of successive dynamical events: first the proton transfers quickly from the chromophore to the acceptor Asp148. Thereafter, on a slower time scale, there are geometrical changes in the cavity of the chromophore that involve the distance between the chromophore and Asp148, the planarity of the excited-state chromophore, and the distance between the chromophore and Tyr145. We find two different non-radiative relaxation channels that are operative for structures in the reactant region and that can explain the mismatch between the decay of the emission of A∗ and the rise of the emission of I∗, as well as the temperature dependence of the non-radiative decay rate.
Original languageEnglish
Pages (from-to)11067-11080
JournalPhysical Chemistry Chemical Physics
Volume20
Issue number16
DOIs
Publication statusPublished - 1 Jan 2018

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