ArticleBiochemistry2014
Molecular mechanism of photoactivation and structural location of the cyanobacterial orange carotenoid protein.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- A Comment on "Deep Proteogenomics of a Photosynthetic Cyanobacterium".Journal of proteome research · 2026Article
- Mass spectrometry reveals the evolutionary conservation of phycobiliprotein complexes.Nature communications · 2026Article
- Light sensitive orange carotenoid proteins (OCPs) in cyanobacterial photoprotection: evolutionary insights, structural-functional dynamics and biotechnological prospects.Archives of microbiology · 2025Review
- Relationship between non-photochemical quenching efficiency and the energy transfer rate from phycobilisomes to photosystem II.Photosynthesis research · 2024Article
- Solution Structures of Two Different FRP-OCP Complexes as Revealed via SEC-SANS.International journal of molecular sciences · 2024Article
- The increasing role of structural proteomics in cyanobacteria.Essays in biochemistry · 2023Review
- Article
- Oligomerization processes limit photoactivation and recovery of the orange carotenoid protein.Biophysical journal · 2022Article
- High-Resolution Native Mass Spectrometry.Chemical reviews · 2022Review
- Carotenoids from Cyanobacteria: Biotechnological Potential and Optimization Strategies.Biomolecules · 2021Review
- Physiological and Transcriptomic Responses to Nitrogen Deficiency inFrontiers in plant science · 2021Article
- Phycobilisomes Harbor FNRmBio · 2019Article
- Single-molecule trapping and spectroscopy reveals photophysical heterogeneity of phycobilisomes quenched by Orange Carotenoid Protein.Nature communications · 2019Article
- OCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria.Nature communications · 2018Article
- Site, trigger, quenching mechanism and recovery of non-photochemical quenching in cyanobacteria: recent updates.Photosynthesis research · 2018Review
- Photoprotective, excited-state quenching mechanisms in diverse photosynthetic organisms.The Journal of biological chemistry · 2018Review
- Photoactivation and relaxation studies on the cyanobacterial orange carotenoid protein in the presence of copper ion.Photosynthesis research · 2018Article
- A functional compartmental model of the Synechocystis PCC 6803 phycobilisome.Photosynthesis research · 2018Article
- Biophysical modeling of in vitro and in vivo processes underlying regulated photoprotective mechanism in cyanobacteria.Photosynthesis research · 2017Article
- Coupled rows of PBS cores and PSII dimers in cyanobacteria: symmetry and structure.Photosynthesis research · 2017Article
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Authors and funding
7 authors.
Funding
Abstract
The orange carotenoid protein (OCP) plays a photoprotective role in cyanobacterial photosynthesis similar to that of nonphotochemical quenching in higher plants. Under high-light conditions, the OCP binds to the phycobilisome (PBS) and reduces the extent of transfer of energy to the photosystems. The protective cycle starts from a light-induced activation of the OCP. Detailed information about the molecular mechanism of this process as well as the subsequent recruitment of the active OCP to the phycobilisome are not known. We report here our investigation on the OCP photoactivation from the cyanobacterium Synechocystis sp. PCC 6803 by using a combination of native electrospray mass spectrometry (MS) and protein cross-linking. We demonstrate that native MS can capture the OCP with its intact pigment and further reveal that the OCP undergoes a dimer-to-monomer transition upon light illumination. The reversion of the activated form of the OCP to the inactive, dark form was also observed by using native MS. Furthermore, in vitro reconstitution of the OCP and PBS allowed us to perform protein chemical cross-linking experiments. Liquid chromatography-MS/MS analysis identified cross-linking species between the OCP and the PBS core components. Our result indicates that the N-terminal domain of the OCP is closely involved in the association with a site formed by two allophycocyanin trimers in the basal cylinders of the phycobilisome core. This report improves our understanding of the activation mechanism of the OCP and the structural binding site of the OCP during the cyanobacterial nonphotochemical quenching process.
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