Photo-isomerization of the isolated photoactive yellow protein chromophore: what comes before the primary step?

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

doi:10.1039/d1cp05259d

Photo-isomerization of the isolated photoactive yellow protein chromophore: what comes before the primary step?

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

Chemistry

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

Abstract

Photoactive proteins typically rely on structural changes in a small chromophore to initiate a biological response. While these changes often involve isomerization as the "primary step", preceding this is an ultrafast relaxation of the molecular framework caused by the sudden change in electronic structure upon photoexcitation. Here, we capture this motion for an isolated model chromophore of the photoactive yellow protein using time-resolved photoelectron imaging. It occurs in <150 fs and is apparent from a spectral shift of ∼70 meV and a change in photoelectron anisotropy. Electronic structure calculations enable the quantitative assignment of the geometric and electronic structure changes to a planar intermediate from which the primary step can then proceed.

Original language	English
Pages (from-to)	1305-1309
Number of pages	5
Journal	Physical chemistry chemical physics : PCCP
Volume	24
Issue number	3
DOIs	https://doi.org/10.1039/d1cp05259d
Publication status	Published - 19 Jan 2022

Keywords

Bacterial Proteins/chemistry
Chromogenic Compounds/chemistry
Coumaric Acids/chemistry
Isomerism
Light
Photochemical Processes/radiation effects
Photoreceptors, Microbial/chemistry

Access to Document

10.1039/d1cp05259d

Cite this

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title = "Photo-isomerization of the isolated photoactive yellow protein chromophore: what comes before the primary step?",

abstract = "Photoactive proteins typically rely on structural changes in a small chromophore to initiate a biological response. While these changes often involve isomerization as the {"}primary step{"}, preceding this is an ultrafast relaxation of the molecular framework caused by the sudden change in electronic structure upon photoexcitation. Here, we capture this motion for an isolated model chromophore of the photoactive yellow protein using time-resolved photoelectron imaging. It occurs in <150 fs and is apparent from a spectral shift of ∼70 meV and a change in photoelectron anisotropy. Electronic structure calculations enable the quantitative assignment of the geometric and electronic structure changes to a planar intermediate from which the primary step can then proceed.",

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language = "English",

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journal = "Physical chemistry chemical physics : PCCP",

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publisher = "The Royal Society of Chemistry",

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T1 - Photo-isomerization of the isolated photoactive yellow protein chromophore

T2 - what comes before the primary step?

AU - Anstöter, Cate S

AU - Curchod, Basile F E

AU - Verlet, Jan R R

PY - 2022/1/19

Y1 - 2022/1/19

N2 - Photoactive proteins typically rely on structural changes in a small chromophore to initiate a biological response. While these changes often involve isomerization as the "primary step", preceding this is an ultrafast relaxation of the molecular framework caused by the sudden change in electronic structure upon photoexcitation. Here, we capture this motion for an isolated model chromophore of the photoactive yellow protein using time-resolved photoelectron imaging. It occurs in <150 fs and is apparent from a spectral shift of ∼70 meV and a change in photoelectron anisotropy. Electronic structure calculations enable the quantitative assignment of the geometric and electronic structure changes to a planar intermediate from which the primary step can then proceed.

AB - Photoactive proteins typically rely on structural changes in a small chromophore to initiate a biological response. While these changes often involve isomerization as the "primary step", preceding this is an ultrafast relaxation of the molecular framework caused by the sudden change in electronic structure upon photoexcitation. Here, we capture this motion for an isolated model chromophore of the photoactive yellow protein using time-resolved photoelectron imaging. It occurs in <150 fs and is apparent from a spectral shift of ∼70 meV and a change in photoelectron anisotropy. Electronic structure calculations enable the quantitative assignment of the geometric and electronic structure changes to a planar intermediate from which the primary step can then proceed.

KW - Bacterial Proteins/chemistry

KW - Chromogenic Compounds/chemistry

KW - Coumaric Acids/chemistry

KW - Isomerism

KW - Light

KW - Photochemical Processes/radiation effects

KW - Photoreceptors, Microbial/chemistry

U2 - 10.1039/d1cp05259d

DO - 10.1039/d1cp05259d

M3 - Article

C2 - 34984423

SN - 1463-9076

VL - 24

SP - 1305

EP - 1309

JO - Physical chemistry chemical physics : PCCP

JF - Physical chemistry chemical physics : PCCP

IS - 3

ER -