Hauska G, Samoray D, Orlich G, Nelson N
Eur J Biochem. 1980 Oct;111(2):535-43. doi: 10.1111/j.1432-1033.1980.tb04969.x.
Photophosphorylation has been reconstituted in a liposomal system containing reaction centers of photosystem I and coupling-factor complex, both highly purified from spinach chloroplasts. This energy-converting model system was put together by diluting the preparation of the coupling-factor complex with an aqueous suspension of proteolipid vesicles, preformed from photosystem-I reaction centers and soybean phospholipids by sonication. In the presence of reduced N-methyl-phenazonium methosulfate the system catalyzed photophosphorylation with rates up to 50 mumol ATP formed x mg chlorophyll-1 x h-1, which was sensitive to uncouplers and to N,N'-dicyclohexyl-carbodiimide. The properties of the system in comparison to chloroplasts is discussed.
光磷酸化作用已在一个脂质体系统中得以重建，该系统包含光系统I的反应中心和偶联因子复合物，二者均从菠菜叶绿体中高度纯化而来。这个能量转换模型系统是通过用蛋白脂质体的水悬浮液稀释偶联因子复合物的制剂而组装起来的，蛋白脂质体是由光系统I反应中心和大豆磷脂通过超声处理预先形成的。在存在还原型N-甲基吩嗪硫酸甲酯的情况下，该系统催化光磷酸化作用，形成ATP的速率高达50 μmol ATP·mg叶绿素⁻¹·h⁻¹，该速率对解偶联剂和N,N'-二环己基碳二亚胺敏感。文中讨论了该系统与叶绿体相比的特性。
