Deckers-Hebestreit G, Altendorf K
Universität Osnabrück, Fachbereich Biologie/Chemie, Arbeitsgruppe Mikrobiologie, Germany.
Annu Rev Microbiol. 1996;50:791-824. doi: 10.1146/annurev.micro.50.1.791.
Membrane-bound ATP synthases (F0F1-ATPases) of bacteria serve two important physiological functions. The enzyme catalyzes the synthesis of ATP from ADP and inorganic phosphate utilizing the energy of an electrochemical ion gradient. On the other hand, under conditions of low driving force, ATP synthases function as ATPases, thereby generating a transmembrane ion gradient at the expense of ATP hydrolysis. The enzyme complex consists of two structurally and functionally distinct parts: the membrane-integrated ion-translocating F0 complex and the peripheral F1 complex, which carries the catalytic sites for ATP synthesis and hydrolysis. The ATP synthase of Escherichia coli, which has been the most intensively studied one, is composed of eight different subunits, five of which belong to F1, subunits alpha, beta, gamma, delta, and epsilon (3:3:1:1:1), and three to F0, subunits a, b, and c (1:2:10 +/- 1). The similar overall structure and the high amino acid sequence homology indicate that the mechanism of ion translocation and catalysis and their mode of coupling is the same in all organisms.
细菌的膜结合ATP合酶（F0F1 - ATP酶）具有两种重要的生理功能。该酶利用电化学离子梯度的能量催化由ADP和无机磷酸合成ATP。另一方面，在驱动力较低的条件下，ATP合酶作为ATP酶发挥作用，从而以ATP水解为代价产生跨膜离子梯度。酶复合物由两个结构和功能不同的部分组成：膜整合的离子转运F0复合物和外周F1复合物，后者带有ATP合成和水解的催化位点。研究最为深入的大肠杆菌ATP合酶由八个不同的亚基组成，其中五个属于F1，即α、β、γ、δ和ε亚基（3:3:1:1:1），三个属于F0，即a、b和c亚基（1:2:10 +/- 1）。相似的整体结构和高氨基酸序列同源性表明，所有生物体中离子转运和催化机制及其偶联模式都是相同的。
