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Resonance Raman spectroscopy of a light-harvesting protein from the brown alga Laminaria saccharina

机译:褐藻海带糖衣藻中一种光收集蛋白的共振拉曼光谱

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摘要

Resonance Raman spectroscopy of an antenna protein from the brown alga Laminaria saccharina has been used to investigate the molecular structure of this light-harvesting complex (LHC) at the level of its bound pigments, chlorophylls (chi) a and c and the xanthophyll fucoxanthin. Evidence has been obtained for the conservation of pigment structure during the isolation procedure used, Six chi a and two chi c molecules are indicated from the positions and relative contributions of stretching modes of their keto-carbonyl groups. Of special interest is the presence of a population of chls a having a protein-binding conformation highly similar to that seen in antenna proteins from higher plants, possibly indicating a common structural motif within this extended gene family. The eight fucoxanthin molecules evidenced are all in the all-trans conformation however, one or two have a highly twisted configuration. The results are discussed in terms of common and varying structural features of LHCs in higher plants and algae. [References: 44]
机译:褐藻海带糖衣藻的触角蛋白的共振拉曼光谱已用于研究该光收集复合物(LHC)在其结合的色素,叶绿素(chi)a和c以及叶黄素岩藻黄质的水平上的分子结构。已经获得了在使用的分离过程中保持颜料结构的证据。从它们的酮-羰基的拉伸方式的位置和相对贡献中可以看出有六个chia和两个chic分子。特别令人感兴趣的是存在具有与高等植物的触角蛋白中高度相似的蛋白结合构象的chls群体,这可能表明该扩展的基因家族具有共同的结构基序。证实的八个岩藻黄质分子全部处于全反式构象,但是,一个或两个具有高度扭曲的构型。根据高等植物和藻类中LHC的共同和变化的结构特征讨论了结果。 [参考:44]

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