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Light‐Controlled Tyrosine Nitration of Proteins
Author(s) -
Long Tengfang,
Liu Lei,
Tao Youqi,
Zhang Wanli,
Quan Jiale,
Zheng Jie,
Hegemann Julian D.,
Uesugi Motonari,
Yao Wenbing,
Tian Hong,
Wang Huan
Publication year - 2021
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.202102287
Subject(s) - tyrosine , nitration , chemistry , nitrotyrosine , biochemistry , thermostability , biophysics , combinatorial chemistry , biology , organic chemistry , enzyme , nitric oxide synthase
Tyrosine nitration of proteins is one of the most important oxidative post‐translational modifications in vivo. A major obstacle for its biochemical and physiological studies is the lack of efficient and chemoselective protein tyrosine nitration reagents. Herein, we report a generalizable strategy for light‐controlled protein tyrosine nitration by employing biocompatible dinitroimidazole reagents. Upon 390 nm irradiation, dinitroimidazoles efficiently convert tyrosine residues into 3‐nitrotyrosine residues in peptides and proteins with fast kinetics and high chemoselectivity under neutral aqueous buffer conditions. The incorporation of 3‐nitrotyrosine residues enhances the thermostability of lasso peptide natural products and endows murine tumor necrosis factor‐α with strong immunogenicity to break self‐tolerance. The light‐controlled time resolution of this method allows the investigation of the impact of tyrosine nitration on the self‐assembly behavior of α‐synuclein.