Abstract
The photoexcited triplet state of the carotenoid peridinin in the peridinin–chlorophyll a–protein (PCP) of the dinoflagellate Heterocapsa pygmaea has been investigated by pulsed electron paramagnetic resonance (EPR) and pulsed electron-nuclear double resonance (ENDOR) spectroscopies. The α- and β-protons hyperfine couplings of the peridinin-conjugated chain have been derived from Davies and Mims ENDOR experiments. The spectroscopic results have been compared to those obtained for the main form of the PCP complex and for the high-salt PCP form from Amphidinium carterae. The EPR features of the peridinin triplet state are very similar in the antenna complexes belonging to the two different dinoflagellate species, proving that the triplet formation pathway and the triplet localization on one specific peridinin per subcluster are common features of different PCP antennas. No significant variation of the hyperfine couplings of the peridinin triplet state has been detected between the main form of the PCP complex from A. carterae and H. pygmaea. The spectroscopic results confirm the close relationship between the Amphidinium PCP and the corresponding Heterocapsa complex at least in terms of mutual arrangement of the chlorophyll a–peridinin pair involved in photoprotection and in terms of conformation of the peridinin-conjugated chain.
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Acknowledgments
This work was supported by the Italian Ministry for University and Research (MURST) under the project PRIN2007. We thank Prof. Giovanni Giacometti for fruitful discussions and advice and Roger Hiller for kindly providing samples of PCP proteins.
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Di Valentin, M., Salvadori, E., Ceola, S. et al. Pulsed EPR and ENDOR on the Peridinin Triplet State Involved in the Photoprotective Mechanism in Peridinin–Chlorophyll a–Proteins. Appl Magn Reson 37, 191 (2010). https://doi.org/10.1007/s00723-009-0046-y
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DOI: https://doi.org/10.1007/s00723-009-0046-y