Pachence J M, Dutton P L, Blasie J K
Biochim Biophys Acta. 1979 Nov 8;548(2):348-73. doi: 10.1016/0005-2728(79)90141-5.
Reaction center protein, isolated from the photosynthetic bacterium Rhodopseudomonas sphaeroides R26 mutant, was incorporated into phosphatidylcholine bilayers forming a homogeneous population of unilamellar vesicles. Cytochrome c, added to preformed reaction center-phosphatidylcholine vesicles, rapidly reduced up to 90% of the laser-generated (BChl)2+ of the reaction center (with kinetics of electron transfer similar to those in the chromatophore membrane) which suggests that the portion of the reaction center which accommodates functional cytochrome c binding sites is exposed predominantly on the exterior of the vesicles. Unit cell electron density profiles were derived from lamellar X-ray diffraction from oriented reaction center-phosphatidylcholine membrane multilayers at varying lipid/protein ratios. The analysis of these profiles showed that the reaction center protein incorporates into the phosphatidylcholine membrane with unique sidedness and that the profile of the reaction center protein itself is asymmetric and spans the membrane.
从光合细菌球形红假单胞菌R26突变体中分离出的反应中心蛋白，被整合到磷脂酰胆碱双层中，形成了均匀的单层囊泡群体。将细胞色素c添加到预先形成的反应中心 - 磷脂酰胆碱囊泡中，它能迅速还原反应中心高达90%的激光产生的（BChl）2+（电子转移动力学与在载色体膜中的相似），这表明容纳功能性细胞色素c结合位点的反应中心部分主要暴露在囊泡的外部。单位晶胞电子密度分布图来自于不同脂质/蛋白质比例下定向的反应中心 - 磷脂酰胆碱膜多层的层状X射线衍射。对这些分布图的分析表明，反应中心蛋白以独特的取向整合到磷脂酰胆碱膜中，并且反应中心蛋白本身的分布图是不对称的且跨越了膜。
