Tyrosine-Specific Chemical Modification with in Situ Hemin-Activated Luminol Derivatives

Shinichi Sato, Kosuke Nakamura, Hiroyuki Nakamura

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54 Citations (Scopus)


Tyrosine-specific chemical modification was achieved using in situ hemin-activated luminol derivatives. Tyrosine residues in peptide and protein were modified effectively with N-methylated luminol derivatives under oxidative conditions in the presence of hemin and H2O2. Both single and double modifications of the tyrosine residue occurred in the reaction of angiotensin II with N-methylated luminol derivative 9. Tyrosine-specific chemical modification of the model protein bovine serum albumin (BSA) revealed that the surface-exposed tyrosine residues were selectively modified with 9. We succeeded in the functionalization of several proteins using azide-conjugated compound 18 using alkyne-conjugated probes by copper(I)-catalyzed azide-alkyne cycloaddition (CuAAC) or dibenzocyclooctyne (DBCO)-mediated copper-free click chemistry. This tyrosine-specific modification was orthogonal to conventional lysine modification by N-hydroxysuccinimide (NHS) ester, and dual functionalization by fluorescence modification of tyrosine residues and PEG modification of lysine residues was achieved without affecting the modification efficiency.

Original languageEnglish
Pages (from-to)2633-2640
Number of pages8
JournalACS Chemical Biology
Issue number11
Publication statusPublished - 2015 Nov 20
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine


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