Kitajima M, Butler W L
Department of Biology, University of California, San Diego, La Jolla, California 92093.
Plant Physiol. 1976 May;57(5):746-50. doi: 10.1104/pp.57.5.746.
Chloroplast and photosystem I particles were encapsulated in small spheres (about 20 mum diameter) with an artificial membrane built up by cross-linking amino groups of protamine with toluenediisocyanate. The artificial membrane was permeable to small substrate and product molecules but not to soluble proteins. Photosystem I activity was retained by the encapsulated chloroplast particles. Washed photosystem I particles were encapsulated with the soluble proteins, ferredoxin, and ferredoxin-NADP oxidoreductase, and the microcapsules photoreduced NADP using ascorbate plus dichlorophenolindophenol as the electron donor. The photosystem I particles were also encapsulated with hydrogenase from Chromatium and a very low rate of photoevolution of hydrogen was obtained. The results show that chloroplast membrane fragments can be encapsulated with soluble proteins that couple transfer reactions to the primary photochemical apparatus.
叶绿体和光系统I颗粒被包裹在小球体（直径约20微米）中，小球体的人工膜是通过将鱼精蛋白的氨基与甲苯二异氰酸酯交联而成。该人工膜对小分子底物和产物分子具有通透性，但对可溶性蛋白质不通透。被包裹的叶绿体颗粒保留了光系统I的活性。将洗涤后的光系统I颗粒与可溶性蛋白质、铁氧化还原蛋白和铁氧化还原蛋白-NADP氧化还原酶一起包裹，这些微胶囊以抗坏血酸加二氯酚靛酚作为电子供体光还原NADP。光系统I颗粒还与来自绿硫菌的氢化酶一起包裹，并获得了非常低的光合放氢速率。结果表明，叶绿体膜片段可以与将转移反应与初级光化学装置偶联的可溶性蛋白质一起被包裹。
