Previous work has shown that tyrosine residues Y423, Y428, and Y432 are potential targets for nitration when tyrosine hydroxylase is exposed to peroxynitrite. For any given protein molecule, up to three nitration events involving these residues may occur. In an effort to determine whether this nitration is directed toward a particular tyrosine residue or randomly distributed among all three tyrosine residues, the goal of this study was to determine whether a singly nitrated molecule was always nitrated at a particular tyrosine residue or whether the initial nitration event was randomly distributed among all three tyrosine residues. Isolation of the singly nitrated peptide V410-E436, followed by subsequent cleavage at D425 and analysis of the resulting peptide fragments by matrix-assisted laser desorption ionization mass spectrometry and LC/MS/MS revealed that the first nitration event was randomly distributed among Y423, Y428, and Y432.
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