Comparison Between the Influences of Phosphatidylcholine and Triton X-100 on the Protein Secondary Structures and Oxygen-evolving Activity of Photosystem Ⅱ  

磷脂酰胆碱和TritonX-100对光系统Ⅱ蛋白二级结构及放氧活性影响的比较(英文)

作　　者：阮翔[1] 许强[1] 毛海滨[1] 单际修[2] 公衍道1张秀芳 匡廷云[2] 赵南明[1] 

机构地区：[1]清华大学生物科学与技术系生物膜与膜生物工程国家重点实验室,北京100084 [2]中国科学院植物研究所光合作用基础研究开放实验室,北京100093

出　　处：《Acta Botanica Sinica》2000年第12期1220-1224,共5页Acta Botanica Sinica（植物学报：英文版）

基　　金：TheStateKeyBasicResearchandDevelopmentPlan (G19980 10 10 0 ) ;theNationalNaturalScienceFoundationofChina .

摘　　要：The structural and functional alterations within the PSⅡ membrane from phosphatidylcholine reconstitution and Triton X_100 (TX_100) treatment were studied by using Fourier transform_infrared (FT_IR) spectroscopic technique and oxygen electrode. Phosphatidylcholine reconstitution showed no significant effect on the protein secondary structures of PSⅡ membrane but an increase of the rate of PSⅡ_mediated oxygen_evolution. The phosphatidylcholine lipids with different length of acyl chains displayed different capabilities to stimulate oxygen_evolution. In contrast, perturbation of the bilayer lipids by TX_100 resulted in obvious changes of the protein secondary structures within the PSⅡ membrane and in the loss of the PSⅡ_mediated oxygen_evolving activity. The results indicate the importance of membrane integrity in maintaining the stability of the photosynthetic membrane proteins.采用傅立叶变换红外光谱技术 (FT_IR)和氧电极研究了磷脂酰胆碱和TritonX_10 0对光系统Ⅱ膜复合物的蛋白二级结构及放氧活性的影响。结果表明 ,磷脂酰胆碱对光系统Ⅱ膜复合物的蛋白二级结构没有显著的影响 ,但能引起放氧活性的提高 ,而且脂酰侧链长度不同 ,对放氧活性的促进程度也不一样。相比较而言 ,TX_10 0对膜脂的扰动却引起蛋白二级结构的明显改变 ,并能抑致放氧活性。结果说明 ,完整的膜结构对维持光合膜蛋白的稳定是非常重要的。

关 键 词：photosystem Ⅱ PHOSPHATIDYLCHOLINE Triton X_100 FT_IR oxygen_evolution 

分 类 号：Q945.11[生物学—植物学]