Pedersen P L
Department of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, Maryland 21205-2185, USA.
J Bioenerg Biomembr. 1996 Oct;28(5):389-95. doi: 10.1007/BF02113979.
How biological systems make ATP has intrigued many scientists for well over half the 20th century, and because of the importance and complexity of the problem it seems likely to continue to be a source of fascination to both senior and younger investigators well into the 21st century. Scientific battles fought to unravel the vast secrets by which ATP synthases work have been fierce, and great victories have been short-lived, tempered with the realization that more structures are needed, additional subunits remain to be conquered, and that during ATP synthesis, not one, but several subunits may undergo either significant conformational changes, repositioning, or perhaps even physical "rotation" similar to bacterial flagella (1,2). In this introductory article, the author briefly summarizes our current knowledge about the complex substructure of ATP synthases, what we have learned from X-ray crystallography of the F1 unit, and current evidence for subunit movements.
在20世纪的大半时间里，生物系统如何产生ATP一直吸引着众多科学家。由于这个问题的重要性和复杂性，在21世纪，它似乎仍将继续吸引资深和年轻的研究人员。为解开ATP合酶工作的巨大秘密而展开的科学斗争十分激烈，重大胜利也是短暂的，因为人们意识到还需要更多的结构，还有更多亚基有待攻克，而且在ATP合成过程中，不止一个亚基，而是几个亚基可能会发生显著的构象变化、重新定位，甚至可能发生类似于细菌鞭毛的物理“旋转”(1,2)。在这篇介绍性文章中，作者简要总结了我们目前对ATP合酶复杂亚结构的了解，我们从F1单元的X射线晶体学中学到了什么，以及目前关于亚基运动的证据。
