Low-temperature time-resolved spectroscopic study of the major light-harvesting complex of Amphidinium carterae
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The major light-harvesting complex of Amphidinium (A.) carterae, chlorophyll-a–chlorophyll-c 2–peridinin–protein complex (acpPC), was studied using ultrafast pump-probe spectroscopy at low temperature (60 K). An efficient peridinin–chlorophyll-a energy transfer was observed. The stimulated emission signal monitored in the near-infrared spectral region was stronger when redder part of peridinin pool was excited, indicating that these peridinins have the S1/ICT (intramolecular charge-transfer) state with significant charge-transfer character. This may lead to enhanced energy transfer efficiency from “red” peridinins to chlorophyll-a. Contrary to the water-soluble antenna of A. carterae, peridinin–chlorophyll-a protein, the energy transfer rates in acpPC were slower under low-temperature conditions. This fact underscores the influence of the protein environment on the excited-state dynamics of pigments and/or the specificity of organization of the two pigment–protein complexes.
KeywordsLight-harvesting Energy transfer Carotenoid Dinoflagellates
The authors thank Miriam Enriquez for help with measuring the absorption spectra at 77 K. The work in Czech Republic was supported by the Czech Science Foundation (P501/12/G055 and P205/11/1164), and project KONTAKT ME09037 from the Ministry of Education of the Czech Republic. Work in the laboratory of HAF was supported by grants from the National Science Foundation (MCB-1243565) and the University of Connecticut Research Foundation.
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