Oligomerization processes limit photoactivation and recovery of the orange carotenoid protein.
Journal
Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626
Informations de publication
Date de publication:
02 08 2022
02 08 2022
Historique:
received:
04
02
2022
revised:
17
05
2022
accepted:
01
07
2022
pubmed:
8
7
2022
medline:
6
8
2022
entrez:
7
7
2022
Statut:
ppublish
Résumé
The orange carotenoid protein (OCP) is a photoactive protein involved in cyanobacterial photoprotection by quenching of the excess of light-harvested energy. The photoactivation mechanism remains elusive, in part due to absence of data pertaining to the timescales over which protein structural changes take place. It also remains unclear whether or not oligomerization of the dark-adapted and light-adapted OCP could play a role in the regulation of its energy-quenching activity. Here, we probed photoinduced structural changes in OCP by a combination of static and time-resolved X-ray scattering and steady-state and transient optical spectroscopy in the visible range. Our results suggest that oligomerization partakes in regulation of the OCP photocycle, with different oligomers slowing down the overall thermal recovery of the dark-adapted state of OCP. They furthermore reveal that upon non-photoproductive excitation a numbed state forms, which remains in a non-photoexcitable structural state for at least ≈0.5 μs after absorption of a first photon.
Identifiants
pubmed: 35794830
pii: S0006-3495(22)00550-1
doi: 10.1016/j.bpj.2022.07.004
pmc: PMC9388578
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Carotenoids
36-88-4
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2849-2872Informations de copyright
Copyright © 2022 Biophysical Society. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.
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