Penefsky H S
Adv Enzymol Relat Areas Mol Biol. 1979;49:223-80. doi: 10.1002/9780470122945.ch6.
Considerable progress has been made in recent years in our understanding of the phosphorylating apparatus in mitochondria, chloroplasts, and bacteria. It has become clear that the structure and the function of the ATP synthesizing apparatus in these widely divergent organisms is similar if not virtually identical. The subunit composition of F1, its molecular architecture, the location and function of substrate binding sites, as well as putative control sites, understanding of the component parts of the oligomycin-sensitive ATPase complex, and the role of these components in the function of the complex all are under active investigation in many laboratories. The developing information and the new insights provided have begun to permit experimental approaches, at the molecular level, to the mode of action of the ATPase in electron-transport-coupled ATP synthesis.
近年来，我们对线粒体、叶绿体和细菌中的磷酸化装置的理解取得了相当大的进展。已经清楚的是，这些差异很大的生物体中ATP合成装置的结构和功能即使不是完全相同，也是相似的。F1的亚基组成、其分子结构、底物结合位点的位置和功能，以及假定的控制位点、对寡霉素敏感的ATP酶复合体组成部分的理解，以及这些组分在复合体功能中的作用，都在许多实验室中进行着积极的研究。所获得的不断发展的信息和新见解已经开始允许在分子水平上对ATP酶在电子传递偶联的ATP合成中的作用方式进行实验研究。
