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Issue 16, 2018
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Ultrafast action chemistry in slow motion: atomistic description of the excitation and fluorescence processes in an archetypal fluorescent protein

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Abstract

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.

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

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Publication details

The article was received on 17 Jan 2018, accepted on 24 Mar 2018 and first published on 26 Mar 2018


Article type: Paper
DOI: 10.1039/C8CP00371H
Citation: Phys. Chem. Chem. Phys., 2018,20, 11067-11080
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    Ultrafast action chemistry in slow motion: atomistic description of the excitation and fluorescence processes in an archetypal fluorescent protein

    P. Armengol, L. Spörkel, R. Gelabert, M. Moreno, W. Thiel and J. M. Lluch, Phys. Chem. Chem. Phys., 2018, 20, 11067
    DOI: 10.1039/C8CP00371H

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