Spotlighting motors and controls of single FoF1-ATP synthase
Spotlighting motors and controls of single FoF1-ATP synthase
复制标题
DOI：
10.1042/bst20130101
复制
发表时间：
2013-10-01
影响因子：
3.9
通讯作者：
Duncan, Thomas M.
中科院分区：
文献类型：
--
作者：
Boersch, Michael;Duncan, Thomas M.
亚基旋转是膜酶FoF1-ATP合成酶催化活性的机械化学中间体。smFRET（单分子FRET）研究提供了对F-1和F-o电机的步长，内部瞬态弹性能量存储和电机控制的见解。为了开发和解释smFRET实验，需要原子结构信息。最近，大肠杆菌酶的F-1结构中含有抑制构象的epsilon亚基，这开启了实时监测epsilon构象变化的研究。本文对smFRET旋转实验进行了总结，并对大肠杆菌中e的c端结构域的构象变化的smFRET新数据进行了概述。
Subunit rotation is the mechanochemical intermediate for the catalytic activity of the membrane enzyme FoF1-ATP synthase. smFRET (single-molecule FRET) studies have provided insights into the step sizes of the F-1 and F-o motors, internal transient elastic energy storage and controls of the motors. To develop and interpret smFRET experiments, atomic structural information is required. The recent F-1 structure of the Escherichia coli enzyme with the epsilon-subunit in an inhibitory conformation initiated a study for real-timemonitoring of the conformational changes of epsilon. The present mini-review summarizes smFRET rotation experiments and previews new smFRET data on the conformational changes of the CTD (C-terminal domain) of e in the E. coli enzyme.