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

被引：11
|
作者：
Slouf, Vaclav [1 ]
Fuciman, Marcel [1 ,2 ]
Johanning, Silke [3 ]
Hofmann, Eckhard [3 ]
Frank, Harry A. [2 ]
Polivka, Tomas [1 ,4 ]
机构：
[1] Univ South Bohemia, Fac Sci, Ceske Budejovice 37005, Czech Republic
[2] Univ Connecticut, Dept Chem, Storrs, CT 06269 USA
[3] Ruhr Univ Bochum, Fac Biol & Biotechnol, Dept Biophys, AG Proteincrystallog, D-44780 Bochum, Germany
[4] Czech Acad Sci, Ctr Biol, Ceske Budejovice 37005, Czech Republic
来源：
PHOTOSYNTHESIS RESEARCH | 2013年 / 117卷 / 1-3期
基金：
美国国家科学基金会;
关键词：
Light-harvesting; Energy transfer; Carotenoid; Dinoflagellates; FUCOXANTHIN-CHLOROPHYLL PROTEIN; EXCITATION-ENERGY TRANSFER; PERIDININ-CHLOROPHYLL; A-PROTEIN; ABSORPTION-SPECTROSCOPY; EXCITED-STATES; DYNAMICS; DINOFLAGELLATE; CAROTENOIDS; SEQUENCE;
D O I：
10.1007/s11120-013-9900-8
中图分类号：
Q94 [植物学];
学科分类号：
071001 ;
摘要：
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 S-1/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.
引用
收藏
页码：257 / 265
页数：9
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