M-Fluorotyrosine (m-Fluoro-DL-tyrosine) may be substituted for tyrosine in the biosynthesis of proteins such as β-galactosidases (Escherichia coli), bacteriorhodopsin and intestinal microvillar enzymes, eg. aminopeptidase N, to study the effect of halogenated tryosines on the proteins properties.
The tracer 6-[18F]fluoro-L-m-tyrosine (FMT) was studied with regard to its biochemistry and kinetics, as well as its utility in evaluating brain dopaminergic function in primates before and after 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) treatment using positron emission tomography (PET). Plasma analysis of FMT
Journal of the American Chemical Society, 128(42), 13654-13655 (2006-10-19)
The complex Re(bpy)(CO)3CN is an excited state oxidant of tyrosine upon deprotonation of the tyrosyl phenol. A series of Re(bpy-FnY)(CO)3CN complexes ([Re]-FnY: [Re]-Y, [Re]-3-FY, [Re]-3,5-F2Y, [Re]-2,3-F2Y, [Re]-2,3,5-F3Y, [Re]-2,3,6-F3Y, and [Re]-F4Y) have been prepared so as to vary the FnY*/FnY- reduction
Journal of biomolecular NMR, 45(3), 255-264 (2009-08-06)
Fluorine NMR is a useful tool to probe protein folding, conformation and local topology owing to the sensitivity of the chemical shift to the local electrostatic environment. As an example we make use of (19)F NMR and 3-fluorotyrosine to evaluate
Crystallographic evidence for isomeric chromophores in 3-fluorotyrosyl-green fluorescent protein.
Jae Hyun Bae et al.
Chembiochem : a European journal of chemical biology, 5(5), 720-722 (2004-05-04)
Expressed protein ligation (EPL) allows semisynthesis of a target protein with site-specific incorporation of probes or unnatural amino acids at its N or C termini. Here, we describe the protocol that our lab has developed for incorporating fluorotyrosines (F(n)Ys) at
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