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Low-temperature time-resolved spectroscopic study of the major light-harvesting complex of Amphidinium carterae
V. Slouf, M. Fuciman, S. Johanning, E. Hofmann, HA. Frank, T. Polívka,
Jazyk angličtina Země Nizozemsko
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
ProQuest Central
od 1997-01-01 do Před 1 rokem
Medline Complete (EBSCOhost)
od 2011-01-01 do Před 1 rokem
Health & Medicine (ProQuest)
od 1997-01-01 do Před 1 rokem
- MeSH
- blízká infračervená spektroskopie * MeSH
- časové faktory 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
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
Citace poskytuje Crossref.org
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