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 twe...

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Bibliographic Details
Published in:Nanoscale 2010-08, Vol.2 (8), p.1284-1293
Main Authors: Shu, Yao-Gen, Yue, Jia-Chang, Ou-Yang, Zhong-Can
Format: Article
Language:English
Subjects:
Biosensing Techniques
Control
Coupling (molecular)
Holoenzymes - chemistry
Holoenzymes - metabolism
Kinetics
Models, Molecular
Motors
Nanocomposites
Nanomaterials
Nanostructure
Proton-Translocating ATPases - chemistry
Proton-Translocating ATPases - metabolism
Rotation
Stators
Translations
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Summary: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 δ -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. A ubiquitous rotary motor in the plasma membrane of bacteria, chloroplasts and mitochondria has been developed into a nanodevice and biosensor.
ISSN:2040-3364
2040-3372
DOI:10.1039/b9nr00411d