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

页码：257 / 265

页数：9

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