The neoxanthin binding site of the major light harvesting complex (LHCII) from higher plants
The neoxanthin binding site of the major light harvesting complex (LHCII) from higher plants
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DOI：
10.1016/s0014-5793(99)00907-2
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发表时间：
1999-07-30
期刊：
影响因子：
3.5
通讯作者：
Bassi, R
中科院分区：
文献类型：
--
作者：
Croce, R;Remelli, R;Bassi, R
叶黄素新黄质在高等植物主要光捕获复合体（LHCII）结构中的定位已通过定点诱变和光谱方法进行了研究。对不同螺旋结构域中的色素结合位点进行的突变分析导致螺旋 C 上突变的新黄质选择性丢失，从而将该色素定位在螺旋 C 和螺旋 A/B 结构域之间。已使用每个多肽结合两个叶黄素分子但缺乏新黄质的重组蛋白来确定新黄质对吸收和线性二色性光谱的贡献。该数据用于推导位于多烯链中的新黄质转变矩的方向，因此确定该方向相对于插入蛋白质的膜平面的法线形成57+/-1.5度的角度。基于这些结果，我们提出了一个尚未解决的 LHCII 结构中类胡萝卜素位点定位模型。 (C) 1999 年欧洲生化学会联合会。
The localisation of the xanthophyll neoxanthin within the structure of the major light harvesting complex (LHCII) of higher plants has been investigated by site-directed mutagenesis and spectroscopic methods. Mutation analysis performed on pigment binding sites in different helix domains leads to selective loss of neoxanthin for mutations on helix C thus localising this pigment between the helix C and helix A/B domains. Recombinant proteins binding two lutein molecules per polypeptide but lacking neoxanthin have been used in order to determine the contribution of neoxanthin to the absorption and linear dichroism spectra. The data were used to derive the orientation of the neoxanthin transition moment, lying in the polyene chain, which was thus determined to form an angle of 57 +/- 1.5 degrees with respect to the normal to the membrane plane where the protein is inserted. On the basis of these results we propose a model for the localisation of the carotenoid site in the LHCII structure which is still unresolved. (C) 1999 Federation of European Biochemical Societies.