ArticlePhotosynthesis research2015
Electronic coupling of the phycobilisome with the orange carotenoid protein and fluorescence quenching.
Article in Photosynthesis research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 33 citations in OpenAlex.
- 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
- Relationship between non-photochemical quenching efficiency and the energy transfer rate from phycobilisomes to photosystem II.Photosynthesis research · 2024Article
- A favorable path to domain separation in the orange carotenoid protein.Protein science : a publication of the Protein Society · 2022Article
- Single-molecule trapping and spectroscopy reveals photophysical heterogeneity of phycobilisomes quenched by Orange Carotenoid Protein.Nature communications · 2019Article
- Site, trigger, quenching mechanism and recovery of non-photochemical quenching in cyanobacteria: recent updates.Photosynthesis research · 2018Review
- A functional compartmental model of the Synechocystis PCC 6803 phycobilisome.Photosynthesis research · 2018Article
- Coupled rows of PBS cores and PSII dimers in cyanobacteria: symmetry and structure.Photosynthesis research · 2017Article
- A Molecular Mechanism for Nonphotochemical Quenching in Cyanobacteria.Biochemistry · 2017Article
- Functions of chromophore-containing domain in the large linker LDoklady. Biochemistry and biophysics · 2016Article
- Orange carotenoid protein burrows into the phycobilisome to provide photoprotection.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
6 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using computational modeling and known 3D structure of proteins, we arrived at a rational spatial model of the orange carotenoid protein (OCP) and phycobilisome (PBS) interaction in the non-photochemical fluorescence quenching. The site of interaction is formed by the central cavity of the OCP monomer in the capacity of a keyhole to the characteristic external tip of the phycobilin-containing domain (PB) and folded loop of the core-membrane linker LCM within the PBS core. The same central protein cavity was shown to be also the site of the OCP and fluorescence recovery protein (FRP) interaction. The revealed geometry of the OCP to the PBLCM attachment is believed to be the most advantageous one as the LCM, being the major terminal PBS fluorescence emitter, gathers, before quenching by OCP, the energy from most other phycobilin chromophores of the PBS. The distance between centers of mass of the OCP carotenoid 3'-hydroxyechinenone (hECN) and the adjacent phycobilin chromophore of the PBLCM was determined to be 24.7 Å. Under the dipole-dipole approximation, from the point of view of the determined mutual orientation and the values of the transition dipole moments and spectral characteristics of interacting chromophores, the time of the direct energy transfer from the phycobilin of PBLCM to the S1 excited state of hECN was semiempirically calculated to be 36 ps, which corresponds to the known experimental data and implies the OCP is a very efficient energy quencher. The complete scheme of OCP and PBS interaction that includes participation of the FRP is proposed.
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