Photoaffinity cross-linking of the coupling factor 1 from Micrococcus luteus by 3'-arylazido-8-azido-ATP.
The vicinity of nucleotide binding sites and the mechanism of ATP synthesis/hydrolysis have been studied with the bifunctional photosensitive ATP analog 3'-arylazido-8-azido-ATP. 3'-Arylazido-8-azido-ATP is hydrolyzed by the F1-ATPase from Micrococcus luteus in the absence of ultraviolet light. Irradiation, by ultraviolet light, of F1-ATPase in the presence of 3'-arylazido-8-azido-ATP results in the specific formation of cross-links between alpha and beta subunits. The results suggest that a hydrolytic nucleotide binding site is located on a beta subunit at or near an alpha subunit, probably at the interface between these subunits. Such a constellation would permit direct subunit-subunit interactions during ATP synthesis/hydrolysis.
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000494:pharmacology; D001386:Azides / Q000494:pharmacology*; D003432:Cross-Linking Reagents / Q000494:pharmacology*; D006868:Hydrolysis; D007700:Kinetics; D008027:Light; D008274:Magnesium / Q000494:pharmacology; D008837:Micrococcus / Q000201:enzymology*; D010782:Photolysis; D006180:Proton-Translocating ATPases / Q000378:metabolism* / Q000528:radiation effects
C026397:3'(O)-(3-(N-(4-azido-2-nitrophenyl)amino)propionyl)-8-azidoadenosine 5'-triphosphate; D001386:Azides; D003432:Cross-Linking Reagents; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases; D008274:Magnesium