Design, synthesis and peroxidase-like activity of 3α-helix proteins covalently bound to heme

Ikuo Obataya, Tomoyuki Kotaki, Seiji Sakamoto, Akihiko Ueno, Hisakazu Mihara

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

As a model of artificial peroxidase, de novo designed three-α-helix proteins, 3α-H9 and 3α-H12, covalently bound to Fe(III)-mesoporphyrin IX were synthesized and examined for a peroxidase-like activity. The activity was regulated according to the positions of His residues in the proteins, and the His residues played a role in an acid-base catalytic function. (C) 2000 Elsevier Science Ltd.

Original languageEnglish
Pages (from-to)2719-2722
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume10
Issue number24
DOIs
Publication statusPublished - 2000 Dec 18

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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