来自大肠杆菌的ATP合酶（F1F0）膜部分（F0）的亚基b对于H+转运以及水溶性F1部分的结合是不可或缺的。
Subunit b of the membrane moiety (F0) of ATP synthase (F1F0) from Escherichia coli is indispensable for H+ translocation and binding of the water-soluble F1 moiety.
作者信息
Schneider E, Altendorf K
出版信息
Proc Natl Acad Sci U S A. 1984 Dec;81(23):7279-83. doi: 10.1073/pnas.81.23.7279.
Abstract
The ATP synthase complex, designated F1F0, of Escherichia coli is composed of a water-soluble portion (F1; membrane-associated ATPase, EC 3.6.1.3) with ATP-hydrolyzing activity and a membrane-integrated part (F0) with H+-translocating activity. F0 is built up from three kinds of subunits (a, b, and c). We have isolated the F0 portion directly from membranes of an E. coli strain (KY 7485) that overproduces the enzyme several fold. Subunit b was extracted from purified F0 by two methods. One method included prolonged incubation of the F0 complex in the presence of trichloroacetate (2.5 M) and the separation of subunit b and an a-c complex by gel filtration. Alternatively, subunit b was extracted by deoxycholate and separated from the a-c complex by hydrophobic-interaction chromatography. Integrated into liposomes, the a-c complex exhibited neither H+ uptake nor binding of F1. However, a functional F0 complex was reconstituted by adding stoichiometric amounts of subunit b to the a-c complex.
摘要
大肠杆菌的ATP合酶复合体，即F1F0，由具有ATP水解活性的水溶性部分（F1；膜结合ATP酶，EC 3.6.1.3）和具有H⁺转运活性的膜整合部分（F0）组成。F0由三种亚基（a、b和c）构成。我们已直接从一株能使该酶过量表达数倍的大肠杆菌菌株（KY 7485）的膜中分离出F0部分。通过两种方法从纯化的F0中提取亚基b。一种方法是在三氯乙酸（2.5 M）存在下将F0复合体长时间温育，然后通过凝胶过滤分离亚基b和a - c复合体。另一种方法是用脱氧胆酸盐提取亚基b，并通过疏水相互作用色谱法将其与a - c复合体分离。整合到脂质体中的a - c复合体既不表现出H⁺摄取，也不表现出与F1的结合。然而，通过向a - c复合体中添加化学计量的亚基b可重建功能性F0复合体。
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