ArticleNature communications2019
Structure of a cyanobacterial photosystem I tetramer revealed by cryo-electron microscopy.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Photosystem I structural fusion with IsiA enhances light-harvesting capabilities of filamentous cyanobacterium during iron deficiency.Cell reports. Physical science · 2026Article
- Antenna photosystem I remodeling in the iron stress-induced complex fromScience advances · 2026Article
- Structural insight of a photosystem I-CpcL-phycobilisome supercomplex from a cyanobacteriumProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structural study of monomeric and dimeric photosystem I-LHCI supercomplexes from a bryophyte.Communications biology · 2026Article
- Light harvesting mechanism of the multi-pigment reaction center with three chlorophyll species adapted to both visible and far-red light.Photosynthesis research · 2026Article
- Photosynthesis under far-red light-evolutionary adaptations and bioengineering of light-harvesting complexes.FEBS letters · 2026Review
- Structural insights into a PSI-ACPI supercomplex from a cryptophyte alga Chroomonas placoidea.Photosynthesis research · 2025Article
- The Photosynthetic Complexes of Thylakoid Membranes of Photoautotrophs and a Quartet of Their Polar Lipids.International journal of molecular sciences · 2025Review
- Improvement of Exciton Hamiltonians for Photosynthetic Reaction Centers by Bayesian Optimization.ACS omega · 2025Article
- Pyridoxine dehydrogenase SePdx regulates photosynthesis via an association with the phycobilisome in a cyanobacterium.The Plant journal : for cell and molecular biology · 2025Article
- Development of a TSR-based method for understanding structural relationships of cofactors and local environments in photosystem I.BMC bioinformatics · 2025Article
- How the Electron-Transfer Cascade is Maintained in Chlorophyll-Biochemistry · 2025Article
- The structural basis for light harvesting in organisms producing phycobiliproteins.The Plant cell · 2024Review
- Presence of low-energy chlorophylls d in photosystem I trimer and monomer cores isolated from Acaryochloris sp. NBRC 102871.Photosynthesis research · 2024Article
- Photosystem I: A Paradigm for Understanding Biological Environmental Adaptation Mechanisms in Cyanobacteria and Algae.International journal of molecular sciences · 2024Review
- Darwin's Green Living Fossil: The MicroalgaMicroorganisms · 2024Article
- Hypothetical chloroplast reading frame 51 encodes a photosystem I assembly factor in cyanobacteria.The Plant cell · 2024Article
- Structures and organizations of PSI-AcpPCI supercomplexes from red tidal and coral symbiotic photosynthetic dinoflagellates.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Isolation and characterization of trimeric and monomeric PSI cores from Acaryochloris marina MBIC11017.Photosynthesis research · 2023Article
- The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis.Nature communications · 2023Article
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Authors and funding
12 authors.
Funding
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Abstract
Photosystem I (PSI) functions to harvest light energy for conversion into chemical energy. The organisation of PSI is variable depending on the species of organism. Here we report the structure of a tetrameric PSI core isolated from a cyanobacterium, Anabaena sp. PCC 7120, analysed by single-particle cryo-electron microscopy (cryo-EM) at 3.3 Å resolution. The PSI tetramer has a C2 symmetry and is organised in a dimer of dimers form. The structure reveals interactions at the dimer-dimer interface and the existence of characteristic pigment orientations and inter-pigment distances within the dimer units that are important for unique excitation energy transfer. In particular, characteristic residues of PsaL are identified to be responsible for the formation of the tetramer. Time-resolved fluorescence analyses showed that the PSI tetramer has an enhanced excitation-energy quenching. These structural and spectroscopic findings provide insights into the physiological significance of the PSI tetramer and evolutionary changes of the PSI organisations.
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