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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 CW, Carbonera D
  • Publication date:
    13/07/2013
  • Journal:
    Biochim Biophys Acta
  • Print ISSN:
    0006-3002
  • PII:
    S0005-2728(13)00120-5
  • Language:
    ENG
  • Keywords:
    Car, Carotenoid, Chl, DFT, Density Functional Theory, EPR, ESE, Electron Spin Echo, FCP, Fucoxanthin, Fx, Hybrid DFT, ISC, LHCII, ODMR, Optically Detected Magnetic Resonance, PCP, QM/QM, QM/QM calculation, 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
  • Addresses:
    Department of Chemical Sciences, University of Padua, via Marzolo 1, 35131 Padova, Italy.
Abstract
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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