Mass mapping sites of nitration in tyrosine hydroxylase

Random vs selective nitration of three tyrosine residues

Chad Borges, Donald M. Kuhn, J. Throck Watson

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)536-540
Number of pages5
JournalChemical Research in Toxicology
Volume16
Issue number4
DOIs
StatePublished - Apr 1 2003
Externally publishedYes

Fingerprint

Nitration
Tyrosine 3-Monooxygenase
Tyrosine
Peptide Fragments
Molecules
Peroxynitrous Acid
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Ionization
Mass spectrometry
Desorption
Peptides
Lasers
Proteins

ASJC Scopus subject areas

  • Drug Discovery
  • Organic Chemistry
  • Chemistry(all)
  • Toxicology
  • Health, Toxicology and Mutagenesis

Cite this

Mass mapping sites of nitration in tyrosine hydroxylase : Random vs selective nitration of three tyrosine residues. / Borges, Chad; Kuhn, Donald M.; Watson, J. Throck.

In: Chemical Research in Toxicology, Vol. 16, No. 4, 01.04.2003, p. 536-540.

Research output: Contribution to journalArticle

@article{e552e773195745dd9d2f263fdc45b405,
title = "Mass mapping sites of nitration in tyrosine hydroxylase: Random vs selective nitration of three tyrosine residues",
abstract = "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.",
author = "Chad Borges and Kuhn, {Donald M.} and Watson, {J. Throck}",
year = "2003",
month = "4",
day = "1",
doi = "10.1021/tx0256681",
language = "English (US)",
volume = "16",
pages = "536--540",
journal = "Chemical Research in Toxicology",
issn = "0893-228X",
publisher = "American Chemical Society",
number = "4",

}

TY - JOUR

T1 - Mass mapping sites of nitration in tyrosine hydroxylase

T2 - Random vs selective nitration of three tyrosine residues

AU - Borges, Chad

AU - Kuhn, Donald M.

AU - Watson, J. Throck

PY - 2003/4/1

Y1 - 2003/4/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0242500752&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0242500752&partnerID=8YFLogxK

U2 - 10.1021/tx0256681

DO - 10.1021/tx0256681

M3 - Article

VL - 16

SP - 536

EP - 540

JO - Chemical Research in Toxicology

JF - Chemical Research in Toxicology

SN - 0893-228X

IS - 4

ER -