TY - JOUR
T1 - Horseradish-Peroxidase-Catalyzed Tyrosine Click Reaction
AU - Sato, Shinichi
AU - Nakamura, Kosuke
AU - Nakamura, Hiroyuki
N1 - Funding Information:
This work was partially supported by a Grant-in-Aid for Scientific Research “Chemical Biology of Natural Products (26102721 to H.N.)”, “Young Scientist (A) (15H05490 to S.S.)” and “Homeostatic regulation by various types of cell death (15H01372 to S.S.)” from MEXT, Japan.
Publisher Copyright:
© 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
PY - 2017/3/2
Y1 - 2017/3/2
N2 - 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).
AB - 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).
KW - heme proteins
KW - horseradish peroxidase
KW - protein labeling
KW - protein modifications
KW - tyrosine modification
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U2 - 10.1002/cbic.201600649
DO - 10.1002/cbic.201600649
M3 - Article
C2 - 28009088
AN - SCOPUS:85010711674
VL - 18
SP - 475
EP - 478
JO - ChemBioChem
JF - ChemBioChem
SN - 1439-4227
IS - 5
ER -