Simidjiev I, Barzda V, Mustárdy L, Garab G
Institute of Plant Biology, Biological Research Center, Hungarian Academy of Sciences, Szeged.
Biochemistry. 1998 Mar 24;37(12):4169-73. doi: 10.1021/bi972726m.
We studied the role of added thylakoid lipids in the light-induced reversible structural changes in isolated macroaggregates of the main light-harvesting chlorophyll a/b complex of photosystem II (LHCII). Loosely stacked lamellar macroaggregates were earlier shown to undergo light-induced reversible structural changes and changes in the photophysical pathways, which resembled those in thylakoid membranes exposed to excess light [Barzda, V., et al. (1996) Biochemistry 35, 8981-8985]. This structural flexibility of LHCII depends critically on the lipid content of the preparations [Simidjiev, I., et al. (1997) Anal. Biochem. 250, 169-175]. It is now reported that lamellar aggregates of LHCII are capable of incorporating substantial amounts of different thylakoid lipids. The long-range order of the chromophores is retained, while the ultrastructure of the lipid-protein macroaggregates can be modified significantly. Addition of thylakoid lipids to the preparations significantly enhances the ability of the LHCII macroaggregates to undergo light-induced structural changes. The lipid environment of the LHCII complexes therefore plays a significant role in determining the structural flexibility of the macroaggregates. As concerns the mechanism of these changes, it is proposed that the absorption of light and the dissipation of its energy in the macrodomains induces thermal fluctuations which bring about changes in the shape or in the stacking interactions of the membranes, this in turn affecting the long-range order of the embedded chromophores. In thylakoids, a similar mechanism is likely to explain the light-induced structural changes which are largely independent of the photochemical activity of the membranes.
我们研究了添加类囊体脂质在光系统II主要捕光叶绿素a/b复合物(LHCII)分离的大聚集体光诱导可逆结构变化中的作用。早期研究表明,松散堆积的层状大聚集体会发生光诱导的可逆结构变化以及光物理途径的改变,这与暴露于过量光下的类囊体膜中的变化相似[Barzda, V., 等人 (1996) Biochemistry 35, 8981 - 8985]。LHCII的这种结构灵活性关键取决于制剂中的脂质含量[Simidjiev, I., 等人 (1997) Anal. Biochem. 250, 169 - 175]。现在有报道称,LHCII的层状聚集体能够掺入大量不同的类囊体脂质。发色团的长程有序性得以保留,而脂蛋白大聚集体的超微结构可被显著改变。向制剂中添加类囊体脂质可显著增强LHCII大聚集体发生光诱导结构变化的能力。因此,LHCII复合物的脂质环境在决定大聚集体的结构灵活性方面起着重要作用。关于这些变化的机制,有人提出,光在宏观区域的吸收及其能量耗散会引发热涨落,进而导致膜的形状或堆积相互作用发生变化,这反过来又会影响嵌入发色团的长程有序性。在类囊体中,类似的机制可能解释了很大程度上独立于膜光化学活性的光诱导结构变化。