- EMDB-54627: Local refinement of a PSI monomer of A. marina NIES-2412 -
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Basic information
Entry
Database: EMDB / ID: EMD-54627
Title
Local refinement of a PSI monomer of A. marina NIES-2412
Map data
Sample
Complex: Photosystem I
Protein or peptide: x 12 types
Ligand: x 9 types
Keywords
Photosystem I / Chlorophyll d / long wavelength / ELECTRON TRANSPORT
Function / homology
Function and homology information
photosystem I reaction center / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / plasma membrane-derived thylakoid membrane / chlorophyll binding / photosynthesis / endomembrane system / 4 iron, 4 sulfur cluster binding / electron transfer activity ...photosystem I reaction center / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / plasma membrane-derived thylakoid membrane / chlorophyll binding / photosynthesis / endomembrane system / 4 iron, 4 sulfur cluster binding / electron transfer activity / oxidoreductase activity / magnesium ion binding / metal ion binding Similarity search - Function
Photosystem I reaction center subunit PsaK / Photosystem I reaction centre subunit PsaK / Photosystem I reaction centre subunit PsaK superfamily / Photosystem I reaction center subunit V/PsaK / Photosystem I psaG / psaK / Photosystem I reaction centre subunit VIII superfamily / Photosystem I PsaF, reaction centre subunit III / Photosystem I PsaF, reaction centre subunit III superfamily / Photosystem I reaction centre subunit III / Photosystem I PsaD ...Photosystem I reaction center subunit PsaK / Photosystem I reaction centre subunit PsaK / Photosystem I reaction centre subunit PsaK superfamily / Photosystem I reaction center subunit V/PsaK / Photosystem I psaG / psaK / Photosystem I reaction centre subunit VIII superfamily / Photosystem I PsaF, reaction centre subunit III / Photosystem I PsaF, reaction centre subunit III superfamily / Photosystem I reaction centre subunit III / Photosystem I PsaD / Photosystem I, reaction centre subunit PsaD superfamily / PsaD / Photosystem I PsaE, reaction centre subunit IV / Photosystem I reaction centre subunit IV / PsaE / Photosystem I PsaJ, reaction centre subunit IX superfamily / Photosystem I PsaJ, reaction centre subunit IX / Photosystem I reaction centre subunit IX / PsaJ / Photosystem I PsaA / Photosystem I protein PsaC / Photosystem I PsaB / Photosystem I PsaA/PsaB, conserved site / Photosystem I psaA and psaB proteins signature. / Photosystem I PsaA/PsaB / Photosystem I PsaA/PsaB superfamily / : / Photosystem I psaA/psaB protein / Electron transport accessory-like domain superfamily / 4Fe-4S dicluster domain / 4Fe-4S ferredoxin, iron-sulphur binding, conserved site / 4Fe-4S ferredoxin-type iron-sulfur binding region signature. / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / 4Fe-4S ferredoxin-type, iron-sulphur binding domain Similarity search - Domain/homology
Photosystem I P700 chlorophyll a apoprotein A2 / Photosystem I reaction center subunit PsaK / Photosystem I P700 chlorophyll a apoprotein A1 / Photosystem I reaction center subunit IV / Photosystem I reaction center subunit II / Psa27 protein / Photosystem I reaction center subunit III / Photosystem I reaction center subunit IX / Photosystem I iron-sulfur center Similarity search - Component
Netherlands, European Union, United Kingdom, 6 items
Organization
Grant number
Country
Netherlands Organisation for Scientific Research (NWO)
714.018.001
Netherlands
European Research Council (ERC)
European Union
Biotechnology and Biological Sciences Research Council (BBSRC)
BB/R001383/1
United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)
BB/V002015/1
United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)
BB/R00921X
United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)
BB/Z516740/1
United Kingdom
Citation
Journal: Sci Adv / Year: 2026 Title: Far-red chlorophyll d clusters extend photosystem I absorption toward the red limit. Authors: Thomas J Oliver / Eduard Elias / Giovanni Consoli / Ho Fong Leong / Violeta Cordón-Preciado / Andrea Fantuzzi / Tanai Cardona / A William Rutherford / Roberta Croce / Abstract: Oxygenic photosynthesis is usually limited to visible light, but the marine cyanobacterium pushes this boundary by harvesting far-red photons with chlorophyll d. The best-studied strain, MBIC11017, ...Oxygenic photosynthesis is usually limited to visible light, but the marine cyanobacterium pushes this boundary by harvesting far-red photons with chlorophyll d. The best-studied strain, MBIC11017, unexpectedly lacks low-energy chlorophylls ("red forms") in photosystem I, limiting absorption beyond 740 nanometers. Here, we show that another strain, NIES-2412, has evolved a strategy to absorb far-red photons up to 760 nanometers. Combining time-resolved fluorescence spectroscopy with cryo-electron microscopy at 2.64-angstrom resolution, we identify two distinct classes of chlorophyll d red forms in its photosystem I. One class originates from classical charge-transfer-exciton mixing, while the other arises purely from excitonic interactions. Mapping all 96 chlorophylls d reveals the precise pigments responsible for these far-red states. We also uncover a previously unreported subunit, PsaX2, which stabilizes the photosystem I complex and shapes pigment geometry and energetics to enable the formation of red forms. Last, we show that the protein modifications responsible for binding and tuning these red forms are widespread across the genus but not within the model MBIC11017 strain. Far-red photons lie close to the energetic limit of oxygenic photosynthesis; their efficient use therefore requires fine-tuning of the photosynthetic machinery. To our knowledge, our findings provide the structural and mechanistic basis of one of the most red-shifted photosystem I complexes identified to date, highlighting a distinct adaptive strategy in far-red light environments and offering design principles for extending photosynthesis in crops into the infrared.
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