Low-temperature time-resolved spectroscopic study of the major light-harvesting complex of Amphidinium carterae
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- blízká infračervená spektroskopie * MeSH
- časové faktory MeSH
- chlorofyl a MeSH
- chlorofyl metabolismus MeSH
- Dinoflagellata metabolismus MeSH
- elektrony MeSH
- karotenoidy metabolismus MeSH
- kinetika MeSH
- nízká teplota * MeSH
- přenos energie MeSH
- světlosběrné proteinové komplexy metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- chlorofyl a MeSH
- chlorofyl MeSH
- karotenoidy MeSH
- peridinin MeSH Prohlížeč
- světlosběrné proteinové komplexy MeSH
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.
Faculty of Science University of South Bohemia Branišovská 31 370 05 České Budějovice Czech Republic
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