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Hydrogen Bonds in Excited State Proton Transfer

D. A. Horke, H. M. Watts, A. D. Smith, E. Jager, E. Springate, O. Alexander, C. Cacho, R. T. Chapman, and R. S. Minns
Phys. Rev. Lett. 117, 163002 – Published 11 October 2016; Erratum Phys. Rev. Lett. 118, 139902 (2017)
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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 noncovalently bound molecules, which stabilizes 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 stabilization 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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  • Received 12 April 2016
  • Corrected 21 March 2017

DOI:https://doi.org/10.1103/PhysRevLett.117.163002

© 2016 American Physical Society

Physics Subject Headings (PhySH)

Atomic, Molecular & Optical

Corrections

21 March 2017

Erratum

Publisher’s Note: Hydrogen Bonds in Excited State Proton Transfer [Phys. Rev. Lett. 117, 163002 (2016)]

D. A. Horke, H. M. Watts, A. D. Smith, E. Jager, E. Springate, O. Alexander, C. Cacho, R. T. Chapman, and R. S. Minns
Phys. Rev. Lett. 118, 139902 (2017)

Synopsis

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Hydrogen Bonding Comes to the Rescue

Published 11 October 2016

Hydrogen bonding may safeguard biomolecules against the damaging effects of UV light.

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Authors & Affiliations

D. A. Horke1,2, H. M. Watts3, A. D. Smith3, E. Jager3, E. Springate4, O. Alexander4, C. Cacho4, R. T. Chapman4, and R. S. Minns3,*

  • 1Center for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany
  • 2The Hamburg Centre for Ultrafast Imaging, University of Hamburg, Luruper Chaussee 149, 22761 Hamburg, Germany
  • 3Chemistry, University of Southampton, Highfield, Southampton SO17 1BJ, United Kingdom
  • 4Central Laser Facility, STFC Rutherford Appleton Laboratory, Didcot, Oxfordshire OX11 0QX, United Kingdom

  • *r.s.minns@soton.ac.uk

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Vol. 117, Iss. 16 — 14 October 2016

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