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Low-temperature time-resolved spectroscopic study of the major light-harvesting complex of Amphidinium carterae

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Abstract

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.

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Acknowledgments

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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Correspondence to Tomáš Polívka.

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Šlouf, V., Fuciman, M., Johanning, S. et al. Low-temperature time-resolved spectroscopic study of the major light-harvesting complex of Amphidinium carterae . Photosynth Res 117, 257–265 (2013). https://doi.org/10.1007/s11120-013-9900-8

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