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Report/Journal Article | PUBDB-2016-03703 |
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2016
APS
College Park, Md.
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Please use a persistent id in citations: doi:10.1103/PhysRevLett.117.163002
Report No.: arXiv:1712.05655
Abstract: Hydrogen bonding interactions between biological chromophores and their surrounding protein and solvent environment significantly affect the photochemical pathways of the chromophore and its biological function. A common first step in the dynamics of these systems is excited state proton transfer between the non-covalently bound molecules, which stabilises the system against dissociation and principally alters relaxation pathways. Despite such fundamental importance, studying excited state proton transfer across a hydrogen bond has proven difficult, leaving uncertainties about the mechanism. Through time-resolved photoelectron imaging measurements we demonstrate how the addition of a single hydrogen bond and the opening of an excited state proton transfer channel dramatically changes the outcome of a photochemical reaction, from rapid dissociation in the isolated chromophore, to efficient stabilisation and ground state recovery in the hydrogen bonded case, and uncover the mechanism of excited state proton transfer at a hydrogen bond, which follows sequential hydrogen and charge transfer processes.
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Preprint/Report
Hydrogen Bonds in Excited State Proton Transfer
College Park, Md. : APS (2016) [10.3204/PUBDB-2017-13720]
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