FoF1-ATPase, rotary motor and biosensor

Abstract

F_oF₁-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 F_o, or F_oF₁ holoenzyme. Magnetic tweezers were employed to manipulate the ATP synthesis/hydrolysis in F₁, and proton translation in F_o. Here, we briefly review our recent works including a systematic kinetics study of the holoenzyme, the mechanochemical coupling mechanism, reconstituting the δ-free F_oF₁-ATPase, direct observation of F_o rotation at single molecule level and activity regulation through external links on the stator.