FoF1-ATPase, rotary motor and biosensor.
F(o)F(1)-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 F(1) and F(o), or F(o)F(1) holoenzyme. Magnetic tweezers were employed to manipulate the ATP synthesis/hydrolysis in F(1), 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 delta-free F(o)F(1)-ATPase, direct observation of F(o) rotation at single molecule level and activity regulation through external links on the stator.
Shu
Yao-Gen
YG
Institute of Theoretical Physics, CAS, Beijing, 100190, China. shuyg@itp.ac.cn
Yue
Jia-Chang
JC
Ou-Yang
Zhong-Can
ZC
D015374:Biosensing Techniques; D020035:Holoenzymes / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism; D012399:Rotation
D020035:Holoenzymes; D006180:Proton-Translocating ATPases