Labeling of peroxide-induced oxidative stress hotspots by hemin-catalyzed tyrosine click

Shinichi Sato, Hiroyuki Nakamura

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

Tyrosyl radical generation is one of the major factors for hemin/peroxide-induced oxidative stress. A method for trapping tyrosyl radical directly was developed using N-methyl luminol derivative, a tyrosine labeling reagent. N-Methyl luminol derivative selectively forms a covalent bond with a tyrosine residue under the single-electron oxidation condition. This reaction labels oxidative stress hotspots not only at the protein level but also at the level of tyrosine residues undergoing oxidation. Human serum albumin complexed with hemin was labeled at Tyr138, the tyrosine residue closest to the hemin binding site and most strongly subjected to oxidative stress caused by hemin/H2O2. Oxidatively damaged proteins were visualized in protein mixtures.

Original languageEnglish
Pages (from-to)885-890
Number of pages6
JournalChemical and Pharmaceutical Bulletin
Volume68
Issue number9
DOIs
Publication statusPublished - 2020 Sep 1

Keywords

  • Albumin
  • Hemin
  • Oxidative stress
  • Peroxide
  • Protein labeling

ASJC Scopus subject areas

  • Chemistry(all)
  • Drug Discovery

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