Effect of protein aggregation on the spectroscopic properties and excited state kinetics of the LHCII pigment-protein complex from green plants

被引：23
|
作者：
Magdaong, Nikki M. [1 ]
Enriquez, Miriam M. [1 ]
LaFountain, Amy M. [1 ]
Rafka, Lauren [1 ]
Frank, Harry A. [1 ]
机构：
[1] Univ Connecticut, Dept Chem, Storrs, CT 06269 USA
来源：
PHOTOSYNTHESIS RESEARCH | 2013年 / 118卷 / 03期
基金：
美国国家科学基金会;
关键词：
Energy transfer; Fluorescence quenching; Light-harvesting; Photosynthesis; Pigment-protein complex; LIGHT-HARVESTING-COMPLEX; PHOTOPROTECTIVE ENERGY-DISSIPATION; FEMTOSECOND TRANSIENT ABSORPTION; TIME-RESOLVED FLUORESCENCE; PHOTOSYSTEM-II; CRYSTAL-STRUCTURE; CHLOROPHYLL FLUORESCENCE; SPECTRAL PROPERTIES; CIRCULAR-DICHROISM; ANTENNA PROTEINS;
D O I：
10.1007/s11120-013-9924-0
中图分类号：
Q94 [植物学];
学科分类号：
071001 ;
摘要：
Steady-state and time-resolved absorption and fluorescence spectroscopic experiments have been carried out at room and cryogenic temperatures on aggregated and unaggregated monomeric and trimeric LHCII complexes isolated from spinach chloroplasts. Protein aggregation has been hypothesized to be one of the mechanistic factors controlling the dissipation of excess photo-excited state energy of chlorophyll during the process known as nonphotochemical quenching. The data obtained from the present experiments reveal the role of protein aggregation on the spectroscopic properties and dynamics of energy transfer and excited state deactivation of the protein-bound chlorophyll and carotenoid pigments.
引用
收藏
页码：259 / 276
页数：18
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