ArticleThe Plant cell2011
In vitro reconstitution of the cyanobacterial photoprotective mechanism mediated by the Orange Carotenoid Protein in Synechocystis PCC 6803.
Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed, 186 citations in OpenAlex.
- Protein/linker dynamics facilitates the structural adaptation of the orange carotenoid protein in cyanobacterial photoprotection: a neutron scattering study.Photosynthesis research · 2026Article
- Structure and quenching of a bundle-shaped phycobilisome.Science advances · 2025Article
- 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
- N-Terminal domain homologs of the orange carotenoid protein increase quenching of cyanobacterial phycobilisomes.Plant physiology · 2025Article
- Two-Photon-Driven Photoprotection Mechanism in Echinenone-Functionalized Orange Carotenoid Protein.Journal of the American Chemical Society · 2025Article
- Elucidating light-induced changes in excitation energy transfer of photosystem I and II in whole cells of two model cyanobacteria.Photosynthesis research · 2025Article
- Light sensitive orange carotenoid proteins (OCPs) in cyanobacterial photoprotection: evolutionary insights, structural-functional dynamics and biotechnological prospects.Archives of microbiology · 2025Review
- Phylogenetic Profiling Analysis of the Phycobilisome Revealed a Novel State-Transition Regulator Gene in Synechocystis sp. PCC 6803.Plant & cell physiology · 2024Article
- MgPhotosynthesis research · 2024Article
- The Orange Carotenoid Protein Triggers Cyanobacterial Photoprotection by Quenching Bilins via a Structural Switch of Its Carotenoid.Journal of the American Chemical Society · 2024Article
- ApcE plays an important role in light-induced excitation energy dissipation in the Synechocystis PCC6803 phycobilisomes.Photosynthesis research · 2024Article
- Roles of ApcD and orange carotenoid protein in photoinduction of electron transport upon dark-light transition in the Synechocystis PCC 6803 mutant deficient in flavodiiron protein Flv1.Photosynthesis research · 2024Article
- Relationship between non-photochemical quenching efficiency and the energy transfer rate from phycobilisomes to photosystem II.Photosynthesis research · 2024Article
- Structure and function of the light-protective orange carotenoid protein families.Current research in structural biology · 2024Review
- Color-Tuning Mechanism of the Lit Form of Orange Carotenoid Protein.Molecules and cells · 2023Article
- Light-induced infrared difference spectroscopy on three different forms of orange carotenoid protein: focus on carotenoid vibrations.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023Article
- Fortuitously compatible protein surfaces primed allosteric control in cyanobacterial photoprotection.Nature ecology & evolution · 2023Article
- Light activation of Orange Carotenoid Protein reveals bicycle-pedal single-bond isomerization.Nature communications · 2022Article
- Is orange carotenoid protein photoactivation a single-photon process?Biophysical reports · 2022Article
- Article
8 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In conditions of fluctuating light, cyanobacteria thermally dissipate excess absorbed energy at the level of the phycobilisome, the light-collecting antenna. The photoactive Orange Carotenoid Protein (OCP) and Fluorescence Recovery Protein (FRP) have essential roles in this mechanism. Absorption of blue-green light converts the stable orange (inactive) OCP form found in darkness into a metastable red (active) form. Using an in vitro reconstituted system, we studied the interactions between OCP, FRP, and phycobilisomes and demonstrated that they are the only elements required for the photoprotective mechanism. In the process, we developed protocols to overcome the effect of high phosphate concentrations, which are needed to maintain the integrity of phycobilisomes, on the photoactivation of the OCP, and on protein interactions. Our experiments demonstrated that, whereas the dark-orange OCP does not bind to phycobilisomes, the binding of only one red photoactivated OCP to the core of the phycobilisome is sufficient to quench all its fluorescence. This binding, which is light independent, stabilizes the red form of OCP. Addition of FRP accelerated fluorescence recovery in darkness by interacting with the red OCP and destabilizing its binding to the phycobilisome. The presence of phycobilisome rods renders the OCP binding stronger and allows the isolation of quenched OCP-phycobilisome complexes. Using the in vitro system we developed, it will now be possible to elucidate the quenching process and the chemical nature of the quencher.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.