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Geometric and electronic structure probed along the isomerisation coordinate of a photoactive yellow protein chromophore

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  • Cate S. Anstöter

    (Durham University)

  • Basile F. E. Curchod

    (Durham University)

  • Jan R. R. Verlet

    (Durham University)

Abstract

Understanding the connection between the motion of the nuclei in a molecule and the rearrangement of its electrons lies at the heart of chemistry. While many experimental methods have been developed to probe either the electronic or the nuclear structure on the timescale of atomic motion, very few have been able to capture both these changes in concert. Here, we use time-resolved photoelectron imaging to probe the isomerisation coordinate on the excited state of an isolated model chromophore anion of the photoactive yellow protein. By probing both the electronic structure changes as well as nuclear dynamics, we are able to uniquely measure isomerisation about a specific bond. Our results demonstrate that the photoelectron signal dispersed in time, energy and angle combined with calculations can track the evolution of both electronic and geometric structure along the adiabatic state, which in turn defines that chemical transformation.

Suggested Citation

  • Cate S. Anstöter & Basile F. E. Curchod & Jan R. R. Verlet, 2020. "Geometric and electronic structure probed along the isomerisation coordinate of a photoactive yellow protein chromophore," Nature Communications, Nature, vol. 11(1), pages 1-7, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16667-x
    DOI: 10.1038/s41467-020-16667-x
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