Ultrafast proton-coupled isomerization in the phototransformation of phytochrome.
Journal
Nature chemistry
ISSN: 1755-4349
Titre abrégé: Nat Chem
Pays: England
ID NLM: 101499734
Informations de publication
Date de publication:
07 2022
07 2022
Historique:
received:
17
10
2019
accepted:
01
04
2022
pubmed:
17
5
2022
medline:
8
7
2022
entrez:
16
5
2022
Statut:
ppublish
Résumé
The biological function of phytochromes is triggered by an ultrafast photoisomerization of the tetrapyrrole chromophore biliverdin between two rings denoted C and D. The mechanism by which this process induces extended structural changes of the protein is unclear. Here we report ultrafast proton-coupled photoisomerization upon excitation of the parent state (Pfr) of bacteriophytochrome Agp2. Transient deprotonation of the chromophore's pyrrole ring D or ring C into a hydrogen-bonded water cluster, revealed by a broad continuum infrared band, is triggered by electronic excitation, coherent oscillations and the sudden electric-field change in the excited state. Subsequently, a dominant fraction of the excited population relaxes back to the Pfr state, while ~35% follows the forward reaction to the photoproduct. A combination of quantum mechanics/molecular mechanics calculations and ultrafast visible and infrared spectroscopies demonstrates how proton-coupled dynamics in the excited state of Pfr leads to a restructured hydrogen-bond environment of early Lumi-F, which is interpreted as a trigger for downstream protein structural changes.
Identifiants
pubmed: 35577919
doi: 10.1038/s41557-022-00944-x
pii: 10.1038/s41557-022-00944-x
pmc: PMC9252900
doi:
Substances chimiques
Bacterial Proteins
0
Protons
0
Phytochrome
11121-56-5
Biliverdine
O9MIA842K9
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
823-830Informations de copyright
© 2022. The Author(s).
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