Kagawa Y, Sone N, Hirata H, Yoshida M
J Bioenerg Biomembr. 1979 Aug;11(3-4):39-78. doi: 10.1007/BF00743196.
(1) Extensive studies on proton-translocating ATPase (H+-ATPase) revealed that H+-ATPase is an energy transforming device universally distributed in membranes of almost all kinds of cells. (2) Crystallization of the catalytic portion (F1) of H+-ATPase showed that F1 is a hexagonal molecule with a central hole. The diameter of F1 is about 90 A and its molecular weight is about 380,000. (3) Use of thermophilic F1 permits the complete reconstitution of F1 from its five subunits (alpha, beta, gamma, delta, epsilon) and demonstration of the gate function of the gamma delta epsilon-complex, the catalytic function of beta (supported by alpha and gamma), and the H+-translocating functions of all five subunits. (4) Studies using purified thermostable F0 showed that F0 is an H+-channel portion of H+-ATPase. The direct measurement of H+-flux through F0, sequencing of DCCD-binding protein, and isolation of F1-binding protein are described. (5) The subunit stoichiometry of F1 may be alpha 3 beta 3 gamma delta epsilon. (6) Reconstitution of stable H+-ATPase-liposomes revealed that ATP is directly synthesized by the flow of H+ driven by an electrochemical potential gradient and that H+ is translocated by ATP hydrolysis. This rules out functions for all the hypothetical components that do not belong to H+-ATPase in H+-driven ATP synthesis. The roles of conformation change and other phenomena in ATP synthesis are also discussed.
(1) 对质子转运ATP酶（H⁺-ATP酶）的广泛研究表明，H⁺-ATP酶是一种能量转换装置，普遍分布于几乎所有类型细胞的膜中。(2) H⁺-ATP酶催化部分（F1）的结晶显示，F1是一个带有中心孔的六边形分子。F1的直径约为90埃，分子量约为380,000。(3) 使用嗜热F1可实现从其五个亚基（α、β、γ、δ、ε）完全重构F1，并证明γδε复合体的门控功能、β的催化功能（由α和γ支持）以及所有五个亚基的H⁺转运功能。(4) 使用纯化的耐热F0进行的研究表明，F0是H⁺-ATP酶的H⁺通道部分。描述了通过F0直接测量H⁺通量、DCCD结合蛋白的测序以及F1结合蛋白的分离。(5) F1的亚基化学计量可能是α₃β₃γδε。(6) 稳定的H⁺-ATP酶-脂质体的重构表明，ATP是由电化学势梯度驱动的H⁺流动直接合成的，并且H⁺通过ATP水解进行转运。这排除了在H⁺驱动的ATP合成中不属于H⁺-ATP酶的所有假设成分的功能。还讨论了构象变化和其他现象在ATP合成中的作用。
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