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Low-temperature time-resolved spectroscopic study of the major light-harvesting complex of Amphidinium carterae |
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| Authors: | Václav Šlouf Marcel Fuciman Silke Johanning Eckhard Hofmann Harry A Frank Tomáš Polívka |
| Institution: | 1. Faculty of Science, University of South Bohemia, Brani?ovská 31, 370 05, ?eské Budějovice, Czech Republic 3. Department of Chemistry, University of Connecticut, 55 North Eagleville Road, Storrs, CT, 06269-3060, USA 2. AG Proteincrystallography, Department of Biophysics, Faculty of Biology and Biotechnology, Ruhr University Bochum, Universit?tsstra?e 150, 44780, Bochum, Germany 4. Biological Centre, Czech Academy of Sciences, Brani?ovská 31, 370 05, ?eské Budějovice, Czech Republic |
| 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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