Asymmetric oxidation catalyzed by myoglobin mutants

Shin Ichi Ozaki, Hui Jun Yang, Toshitaka Matsui, Yoshio Goto, Yoshihito Watanabe

研究成果: Article査読

54 被引用数 (Scopus)

抄録

The sperm whale myoglobin active site mutants (L29H/H64L and F43H/H64L Mb) have been shown to catalyze the asymmetric oxidation of sulfides and olefins. Thioanisole, ethyl phenyl sulfide, and cis-β-methylstyrene are oxidized by L29H/H64L Mb with more than 95% enantiomeric excess (% ee). On the other hand, the F43H/H64L mutant transforms trans-β-methylstyrene into the trans-epoxide with 96% ee. The dominant sulfoxide product in the incubation of alkyl phenyl thioethers is the R isomer; however, the mutants afford dominantly the S isomer of aromatic bicyclic sulfoxides. The results help us to rationalize the difference in the preferred stereochemistry of the Mb mutant-catalyzed reactions. Furthermore, the Mb mutants exhibit an improvement in the oxidation rate up to 300-fold with respect to wild type.

本文言語English
ページ(範囲)183-192
ページ数10
ジャーナルTetrahedron Asymmetry
10
1
DOI
出版ステータスPublished - 1999 1 15
外部発表はい

ASJC Scopus subject areas

  • Catalysis
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

フィンガープリント 「Asymmetric oxidation catalyzed by myoglobin mutants」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル