4.6 Article

Confronting FCP structure with ultrafast spectroscopy data: evidence for structural variations

期刊

PHYSICAL CHEMISTRY CHEMICAL PHYSICS
卷 23, 期 2, 页码 806-821

出版社

ROYAL SOC CHEMISTRY
DOI: 10.1039/d0cp05578f

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资金

  1. Laserlab Europe
  2. Research Council of Lithuania (LMT) [S-MIP-20-44]
  3. Gilibert project [S-LZ-19-3]
  4. Deutsche Forschungsgemeinschaft (DFG) [Bu812/10-1]
  5. European Unions Horizon 2020 research and innovation programme under the Marie Sklodowska-Curie grant [675006]
  6. Young Scientist Scholarship from the Lithuanian Academy of Sciences

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Diatoms are a significant group of algae contributing a quarter of the global primary production. Recent structural studies on FCP complexes have provided insights, but there are discrepancies with ultrafast spectroscopy results. Researchers have developed a trimer-based FCP model for Cyclotella meneghiniana based on available structures and electron microscopy data.
Diatoms are a major group of algae, responsible for a quarter of the global primary production on our planet. Their adaptation to marine environments is ensured by their light-harvesting antenna - the fucoxanthin-chlorophyll protein (FCP) complex, which absorbs strongly in the blue-green spectral region. Although these essential proteins have been the subject of many studies, for a long time their comprehensive description was not possible in the absence of structural data. Last year, the 3D structures of several FCP complexes were revealed. The structure of an FCP dimer was resolved by crystallography for the pennate diatom Phaeodactylum tricornutum [W. Wang et al., Science, 2019, 363, 6427] and the structure of the PSII supercomplex from the centric diatom Chaetoceros gracilis, containing several FCPs, was obtained by electron microscopy [X. Pi et al., Science, 2019, 365, 6452; R. Nagao et al., Nat. Plants, 2019, 5, 890]. In this Perspective article, we evaluate how precisely these structures may account for previously published ultrafast spectroscopy results, describing the excitation energy transfer in the FCP from another centric diatom Cyclotella meneghiniana. Surprisingly, we find that the published FCP structures cannot explain several observations obtained from ultrafast spectroscopy. Using the available structures, and results from electron microscopy, we construct a trimer-based FCP model for Cyclotella meneghiniana, consistent with ultrafast experimental data. As a whole, our observations suggest that the structures from the proteins belonging to the FCP family display larger variations than the equivalent LHC proteins in plants, which may reflect species-specific adaptations or original strategies for adapting to rapidly changing marine environments.

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