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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,
Language English Country Netherlands
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
ProQuest Central
from 1997-01-01 to 1 year ago
Medline Complete (EBSCOhost)
from 2011-01-01 to 1 year ago
Health & Medicine (ProQuest)
from 1997-01-01 to 1 year ago
- MeSH
- Spectroscopy, Near-Infrared * MeSH
- Time Factors MeSH
- Chlorophyll metabolism MeSH
- Dinoflagellida metabolism MeSH
- Electrons MeSH
- Carotenoids metabolism MeSH
- Kinetics MeSH
- Cold Temperature * MeSH
- Energy Transfer MeSH
- Light-Harvesting Protein Complexes metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't 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
References provided by Crossref.org
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