Compound I of heme oxygenase cannot hydroxylate its heme meso-carbon

Toshitaka Matsui, Sun Hee Kim, Hiromichi Jin, Brian M. Hoffman, Masao Ikeda-Saito

研究成果: Article査読

28 被引用数 (Scopus)

抄録

Heme oxygenase (HO) catalyzes heme catabolism through three successive oxygenation steps where the substrate heme itself activates O2. It has been thought that the reactive species responsible for the first heme oxygenation, meso-hydroxylation, is the hydroperoxy-ferric heme intermediate (Fe-OOH) rather than an oxo ferryl porphyrin cation radical, so-called compound I. A recent theoretical study (Kamachi, T.; Yoshizawa, K. J. Am. Chem. Soc. 2005, 127, 10686), however, proposed that compound I can oxidize its meso-carbon atom with the assistance of a bridging water molecule. In this communication, we report the first direct observation of compound I of a heme-HO-1 complex, generated by reaction of ferric-HO-1 with m-chloroperbenzoic acid. HO compound I slowly decays to compound II without producing any meso-hydroxylated products. It does react with guaiacol and thioanisole, however. Our findings unambiguously rule out involvement of compound I in the HO catalysis.

本文言語English
ページ(範囲)1090-1091
ページ数2
ジャーナルJournal of the American Chemical Society
128
4
DOI
出版ステータスPublished - 2006 2 1

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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