ArticlePhotosynthesis research2017
Coupled rows of PBS cores and PSII dimers in cyanobacteria: symmetry and structure.
Article in Photosynthesis research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 20 citations in OpenAlex.
- Relationship between non-photochemical quenching efficiency and the energy transfer rate from phycobilisomes to photosystem II.Photosynthesis research · 2024Article
- Structure of a dimeric photosystem II complex from a cyanobacterium acclimated to far-red light.The Journal of biological chemistry · 2023Article
- Native architecture and acclimation of photosynthetic membranes in a fast-growing cyanobacterium.Plant physiology · 2022Article
- The Role of Selected Wavelengths of Light in the Activity of Photosystem II inInternational journal of molecular sciences · 2021Article
- Structural variability, coordination and adaptation of a native photosynthetic machinery.Nature plants · 2020Article
- Complementary chromatic and far-red photoacclimations in Synechococcus ATCC 29403 (PCC 7335). I: The phycobilisomes, a proteomic approach.Photosynthesis research · 2018Article
- Spectrally decomposed dark-to-light transitions in Synechocystis sp. PCC 6803.Photosynthesis research · 2018Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phycobilisome (PBS) is a giant water-soluble photosynthetic antenna transferring the energy of absorbed light mainly to the photosystem II (PSII) in cyanobacteria. Under the low light conditions, PBSs and PSII dimers form coupled rows where each PBS is attached to the cytoplasmic surface of PSII dimer, and PBSs come into contact with their face surfaces (state 1). The model structure of the PBS core that we have developed earlier by comparison and combination of different fine allophycocyanin crystals, as reported in Zlenko et al. (Photosynth Res 130(1):347-356, 2016b), provides a natural way of the PBS core face-to-face stacking. According to our model, the structure of the protein-protein contact between the neighboring PBS cores in the rows is the same as the contact between the APC hexamers inside the PBS core. As a result, the rates of energy transfer between the cores can occur, and the row of PBS cores acts as an integral PBS "supercore" providing energy transfer between the individual PBS cores. The PBS cores row pitch in our elaborated model (12.4 nm) is very close to the PSII dimers row pitch obtained by the electron microscopy (12.2 nm) that allowed to unite a model of the PBS cores row with a model of the PSII dimers row. Analyzing the resulting model, we have determined the most probable locations of ApcD and ApcE terminal emitter subunits inside the bottom PBS core cylinders and also revealed the chlorophyll molecules of PSII gathering energy from the PBS.
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