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

0425934 - BC 2014 RIV NL eng J - Článek v odborném periodiku
Šlouf, V. - Fuciman, M. - Johanning, S. - Hofmann, E. - Frank, H.A. - Polívka, Tomáš
Low-temperature time-resolved spectroscopic study of the major light-harvesting complex of Amphidinium carterae.
Photosynthesis Research. Roč. 117, 1-3 (2013), s. 257-265. ISSN 0166-8595. E-ISSN 1573-5079
Grant CEP: GA ČR(CZ) GAP205/11/1164
Institucionální podpora: RVO:60077344
Klíčová slova: Dinoflagellates * Energy transfer * Light-harvesting * Carotenoid
Kód oboru RIV: BO - Biofyzika
Impakt faktor: 3.185, rok: 2013

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.
Trvalý link: http://hdl.handle.net/11104/0231744