10833274 |
Lee HW, Sohn JH, Yeh BI, Choi JW, Jung S, Kim HW: 19F NMR investigation of F (1)-ATPase of Escherichia coli using fluorotryptophan labeling. J Biochem. 2000 Jun;127(6):1053-6. Growth of Escherichia coli in the presence of glyphosate, an inhibitor of aromatic amino acid biosynthesis, has permitted the production of proton-dislocating ATPase that is specifically labeled with 5-fluorotryptophan. Five sets of (19) F resonances could be assigned to each tryptophan residue by lauryldimethylamine oxide and carboxypeptidase treatment. On labeling with 4-chloro-7-nitro-benzofurazan, the label attached to b155Lys, which is known to be in the catalytic site, which caused one of the residues, b108Trp, to become nonequivalent. (19) F NMR spectroscopic investigation of internally fluorotryptophan-labeled F (1)-ATPase will provide valuable information about the asymmetric nature of F (1)-ATPase and the conformational changes induced by ligand binding. |
3(0,0,0,3) |