Horseradish-Peroxidase-Catalyzed Tyrosine Click Reaction

Shinichi Sato, Kosuke Nakamura, Hiroyuki Nakamura

Research output: Contribution to journalArticlepeer-review

38 Citations (Scopus)


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 H2O2, 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 H2O2 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, H2O2-free conditions).

Original languageEnglish
Pages (from-to)475-478
Number of pages4
Issue number5
Publication statusPublished - 2017 Mar 2


  • heme proteins
  • horseradish peroxidase
  • protein labeling
  • protein modifications
  • tyrosine modification


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