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

Cate S Anstöter; Basile F E Curchod; Jan R R Verlet

doi:10.1038/s41467-020-16667-x

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

Cate S Anstöter, Basile F E Curchod, Jan R R Verlet

Chemistry

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	2827
Number of pages	7
Journal	Nature Communications
Volume	11
Issue number	1
DOIs	https://doi.org/10.1038/s41467-020-16667-x
Publication status	Published - 4 Jun 2020

Keywords

Anisotropy
Bacterial Proteins/chemistry
Electrons
Isomerism
Photoreceptors, Microbial/chemistry
Time Factors

Access to Document

10.1038/s41467-020-16667-xLicence: CC BY

Cite this

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title = "Geometric and electronic structure probed along the isomerisation coordinate of a photoactive yellow protein chromophore",

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.",

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AU - Anstöter, Cate S

AU - Curchod, Basile F E

AU - Verlet, Jan R R

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AB - 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.

KW - Anisotropy

KW - Bacterial Proteins/chemistry

KW - Electrons

KW - Isomerism

KW - Photoreceptors, Microbial/chemistry

KW - Time Factors

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DO - 10.1038/s41467-020-16667-x

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