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Horseradish‐Peroxidase‐Catalyzed Tyrosine Click Reaction
Author(s) -
Sato Shinichi,
Nakamura Kosuke,
Nakamura Hiroyuki
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201600649
Subject(s) - horseradish peroxidase , hemin , chemistry , tyrosine , oxidative phosphorylation , peroxidase , cysteine , catalysis , biochemistry , combinatorial chemistry , click chemistry , redox , enzyme , organic chemistry , heme
Abstract The efficiency of protein chemical modification on tyrosine residues with N ‐methylluminol derivatives was drastically improved by using horseradish peroxidase (HRP). In the previous method, based on the use of hemin and H 2 O 2 , oxidative side reactions such as cysteine oxidation were problematic for functionalization of proteins selectively on tyrosine residues. Oxidative activation of N ‐methylluminol derivatives with a minimum amount of H 2 O 2 prevented the occurrence of oxidative side reactions under HRP‐catalyzed conditions. As probes for HRP‐catalyzed protein modification, N ‐methylluminol derivatives showed much higher efficiency than tyramide without inducing oligomerization of probe molecules. Tyrosine modification also proceeded in the presence of β‐nicotinamide adenine dinucleotide (NADH, H 2 O 2 ‐free conditions).