ArticleNature communications2022
Structural basis for different types of hetero-tetrameric light-harvesting complexes in a diatom PSII-FCPII supercomplex.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 49 citations in OpenAlex.
- Spectroscopic Investigation of the In Vivo Light-Dependent Photodynamics of the Marine Diatom Phaeodactylum tricornutum.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Cryo-EM structure of photosystem II supercomplex from a green microalga with extreme phototolerance.Nature communications · 2026Article
- Exciton Delocalization Promotes Far-Red Absorption in a Tetrameric ChlorophyllJournal of the American Chemical Society · 2025Article
- Conformational plasticity enables functional switching in diatom light-harvesting complexes.Communications chemistry · 2025Article
- Photosystem II: commonality and diversity with emphasis on the extrinsic subunits.Plant & cell physiology · 2025Review
- Applying an Anti-Kasha Model Resolves Differences Between Photosynthetic and Artificial Pigments.The journal of physical chemistry. B · 2025Article
- Structure of a photosystem II-FCPII supercomplex from a haptophyte reveals a distinct antenna organization.Nature communications · 2025Article
- Chlorophyll Pigments and Their Synthetic Analogs.Plant & cell physiology · 2025Review
- Light harvesting and photoprotective states in the marine diatomRSC advances · 2025Article
- Distribution, Biosynthesis, and Function of Carotenoids in Oxygenic Phototrophic Algae.Marine drugs · 2025Review
- An Unexpected Water Channel in the Light-Harvesting Complex of a Diatom: Implications for the Switch between Light Harvesting and Photoprotection.ACS physical chemistry Au · 2025Article
- Structural and spectroscopic insights into fucoxanthin chlorophyll a/c-binding proteins of diatoms in diverse oligomeric states.Plant communications · 2024Article
- Unraveling the evolutionary trajectory of LHCI in red-lineage algae: Conservation, diversification, and neolocalization.iScience · 2024Article
- Structure of cryptophyte photosystem II-light-harvesting antennae supercomplex.Nature communications · 2024Article
- Structure and distinct supramolecular organization of a PSII-ACPII dimer from a cryptophyte alga Chroomonas placoidea.Nature communications · 2024Article
- Structure of a unique PSII-Pcb tetrameric megacomplex in a chlorophyllScience advances · 2024Article
- Structural insights into photosystem II supercomplex and trimeric FCP antennae of a centric diatom Cyclotella meneghiniana.Nature communications · 2023Article
- Structure of a diatom photosystem II supercomplex containing a member of Lhcx family and dimeric FCPII.Science advances · 2023Article
- Mechanism of Absorption Wavelength Shift Depending on the Protonation State of the Acrylate Group in ChlorophyllThe journal of physical chemistry. B · 2023Article
- Influence of reduced amounts of sulfoquinovosyl diacylglycerol on the thylakoid membranes of the diatomPhotosynthetica · 2023Article
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fucoxanthin chlorophyll (Chl) a/c-binding proteins (FCPs) function as light harvesters in diatoms. The structure of a diatom photosystem II-FCPII (PSII-FCPII) supercomplex have been solved by cryo-electron microscopy (cryo-EM) previously; however, the FCPII subunits that constitute the FCPII tetramers and monomers are not identified individually due to their low resolutions. Here, we report a 2.5 Å resolution structure of the PSII-FCPII supercomplex using cryo-EM. Two types of tetrameric FCPs, S-tetramer, and M-tetramer, are identified as different types of hetero-tetrameric complexes. In addition, three FCP monomers, m1, m2, and m3, are assigned to different gene products of FCP. The present structure also identifies the positions of most Chls c and diadinoxanthins, which form a complicated pigment network. Excitation-energy transfer from FCPII to PSII is revealed by time-resolved fluorescence spectroscopy. These structural and spectroscopic findings provide insights into an assembly model of FCPII and its excitation-energy transfer and quenching processes.
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