Optical control of ultrafast structural dynamics in a fluorescent protein.
Journal
Nature chemistry
ISSN: 1755-4349
Titre abrégé: Nat Chem
Pays: England
ID NLM: 101499734
Informations de publication
Date de publication:
Nov 2023
Nov 2023
Historique:
received:
11
11
2021
accepted:
12
06
2023
medline:
6
11
2023
pubmed:
11
8
2023
entrez:
10
8
2023
Statut:
ppublish
Résumé
The photoisomerization reaction of a fluorescent protein chromophore occurs on the ultrafast timescale. The structural dynamics that result from femtosecond optical excitation have contributions from vibrational and electronic processes and from reaction dynamics that involve the crossing through a conical intersection. The creation and progression of the ultrafast structural dynamics strongly depends on optical and molecular parameters. When using X-ray crystallography as a probe of ultrafast dynamics, the origin of the observed nuclear motions is not known. Now, high-resolution pump-probe X-ray crystallography reveals complex sub-ångström, ultrafast motions and hydrogen-bonding rearrangements in the active site of a fluorescent protein. However, we demonstrate that the measured motions are not part of the photoisomerization reaction but instead arise from impulsively driven coherent vibrational processes in the electronic ground state. A coherent-control experiment using a two-colour and two-pulse optical excitation strongly amplifies the X-ray crystallographic difference density, while it fully depletes the photoisomerization process. A coherent control mechanism was tested and confirmed the wave packets assignment.
Identifiants
pubmed: 37563326
doi: 10.1038/s41557-023-01275-1
pii: 10.1038/s41557-023-01275-1
pmc: PMC10624617
doi:
Substances chimiques
Rhodopsin
9009-81-8
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1607-1615Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM118044
Pays : United States
Informations de copyright
© 2023. The Author(s).
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