FoF1-ATPase, rotary motor and biosensor

摘要

FoF1-ATPase is an amazing molecular rotary motor at the nanoscale. Single molecule technologies have contributed much to the understanding of the motor. For example, fluorescence imaging and spectroscopy revealed the physical rotation of isolated F1 and Fo, orFoF1 holoenzyme. Magnetic tweezers were employed to manipulate the ATP synthesis/hydrolysis in F1 and proton translation in Fo. Here, we briefly review our recent works including a systematic kinetics study of the holoenzyme, the mechanochemical coupling mechanism, reconstituting the <5-free FoF1-ATPase, direct observation of Fo rotation at single molecule level and activity regulation through external links on the stator.