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Publication Detail
Triplet-triplet energy transfer in fucoxanthin-chlorophyll protein from diatom Cyclotella meneghiniana: insights into the structure of the complex.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Di Valentin M, Meneghin E, Orian L, Polimeno A, Büchel C, Salvadori E, Kay CWM, Carbonera D
  • Publication date:
  • Pagination:
    1226, 1234
  • Journal:
    Biochim Biophys Acta
  • Volume:
  • Issue:
  • Status:
  • Country:
  • Print ISSN:
  • PII:
  • Language:
  • Keywords:
    Car, Carotenoid, Chl, DFT, Density Functional Theory, EPR, ESE, Electron Spin Echo, FCP, Fucoxanthin, Fx, ISC, LHCII, ODMR, Optically Detected Magnetic Resonance, PCP, QM/QM, TR-EPR, TTET, Time Resolved Electron Paramagnetic Resonance, Triplet state, ZFS, carotenoid, chlorophyll, fucoxanthin, fucoxanthin chlorophyll protein, intersystem crossing, light harvesting complex II, peridinin–chlorophyll–protein, quantum mechanics/quantum mechanics, triplet–triplet energy transfer, zero field splitting, Chlorophyll, Chlorophyll Binding Proteins, Diatoms, Electron Spin Resonance Spectroscopy, Energy Transfer, Light, Xanthophylls
Although the major light harvesting complexes of diatoms, called FCPs (fucoxanthin chlorophyll a/c binding proteins), are related to the cab proteins of higher plants, the structures of these light harvesting protein complexes are much less characterized. Here, a structural/functional model for the "core" of FCP, based on the sequence homology with LHCII, in which two fucoxanthins replace the central luteins and act as quenchers of the Chl a triplet states, is proposed. Combining the information obtained by time-resolved EPR spectroscopy on the triplet states populated under illumination, with quantum mechanical calculations, we discuss the chlorophyll triplet quenching in terms of the geometry of the chlorophyll-carotenoid pairs participating to the process. The results show that local structural rearrangements occur in FCP, with respect to LHCII, in the photoprotective site.
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