F0F1-ATPase activity regulated by external links on beta subunits.
F(o)F(1)-ATPase activity is regulated by external links on beta subunits with different molecular weight. It is inhibited when anti-beta subunit antibody, streptavidin and H9 antibody link on the beta subunits successively, but is activated when virus was binded. Western blotting indicated that the employed anti-beta antibody target was on the non-catalytic site of the beta subunit. Furthermore, an ESR study of spin-labeled ATP (SL-ATP) showed that the affinity of ATP to the holoenzyme increases with increasing external links on the beta subunits. This simple regulation method may have great potential in the design of rapid, free labeled, sensitive and selective biosensors.
Cheng
Jie
J
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Zhang
Xiao-ai
XA
Shu
Yao-Gen
YG
Yue
Jia-Chang
JC
D000255:Adenosine Triphosphate / Q000737:chemistry; D000911:Antibodies, Monoclonal / Q000276:immunology; D015374:Biosensing Techniques; D020134:Catalytic Domain; D004578:Electron Spin Resonance Spectroscopy; D020035:Holoenzymes / Q000737:chemistry / Q000276:immunology; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry / Q000276:immunology; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000276:immunology; D013113:Spin Labels
D000911:Antibodies, Monoclonal; D020035:Holoenzymes; D021122:Protein Subunits; D013113:Spin Labels; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases