Labeling of Peroxide-Induced Oxidative Stress Hotspots by Hemin-Catalyzed Tyrosine Click

• Sato Shinichi

  Frontier Research Institute for Interdisciplinary Sciences, Tohoku University Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology

• Nakamura Hiroyuki

  Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology

抄録

Tyrosyl radical generation is one of the major factors for hemin/peroxide-induced oxidative stress. A method for trapping tyrosyl radical directly was developed using N-methyl luminol derivative, a tyrosine labeling reagent. N-Methyl luminol derivative selectively forms a covalent bond with a tyrosine residue under the single-electron oxidation condition. This reaction labels oxidative stress hotspots not only at the protein level but also at the level of tyrosine residues undergoing oxidation. Human serum albumin complexed with hemin was labeled at Tyr138, the tyrosine residue closest to the hemin binding site and most strongly subjected to oxidative stress caused by hemin/H₂O₂. Oxidatively damaged proteins were visualized in protein mixtures.

収録刊行物

• ＣＨＥＭＩＣＡＬ　＆　ＰＨＡＲＭＡＣＥＵＴＩＣＡＬ　ＢＵＬＬＥＴＩＮ

  ＣＨＥＭＩＣＡＬ　＆　ＰＨＡＲＭＡＣＥＵＴＩＣＡＬ　ＢＵＬＬＥＴＩＮ 68 (9), 885-890, 2020-09-01

  公益社団法人 日本薬学会

キーワード

• oxidative stress
• hemin
• protein labeling
• albumin
• peroxide

詳細情報

• CRID: 1390003825209714688
• NII論文ID: 130007893822
• NII書誌ID: AA00602100
• DOI: 10.1248/cpb.c20-00434
• ISSN: 13475223
• ISSN: 00092363
• NDL書誌ID: 030606007
• PubMed: 32879229
• Web Site: http://id.ndl.go.jp/bib/030606007
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I030606007
• Web Site: https://www.jstage.jst.go.jp/article/cpb/68/9/68_c20-00434/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/2021209627
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
  • KAKEN
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