ArticleBiophysical journal2022
Oligomerization processes limit photoactivation and recovery of the orange carotenoid protein.
Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- A light-triggered Time-Resolved X-ray Solution Scattering (TR-XSS) workflow with application to protein conformational dynamics.FEBS open bio · 2026Article
- Optimizing photoexcitation conditions for time-resolved X-ray solution scattering experiments.FEBS open bio · 2026Article
- Time-resolved x-ray solution scattering from detergent solubilized visual rhodopsin.Biophysical journal · 2026Article
- Protein/linker dynamics facilitates the structural adaptation of the orange carotenoid protein in cyanobacterial photoprotection: a neutron scattering study.Photosynthesis research · 2026Article
- Phycobilisome core architecture influences photoprotective quenching by the Orange Carotenoid Protein.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Two-Photon-Driven Photoprotection Mechanism in Echinenone-Functionalized Orange Carotenoid Protein.Journal of the American Chemical Society · 2025Article
- Solution Structures of Two Different FRP-OCP Complexes as Revealed via SEC-SANS.International journal of molecular sciences · 2024Article
- Recent Progress in Solution Structure Studies of Photosynthetic Proteins Using Small-Angle Scattering Methods.Molecules (Basel, Switzerland) · 2023Review
- Is orange carotenoid protein photoactivation a single-photon process?Biophysical reports · 2022Article
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Authors and funding
14 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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