Functional Conversion of Myoglobin Bound to Synthetic Bilayer Membranes: From Dioxygen Storage Protein to Redox Enzyme

Itaru Hamachi, Shunsaku Noda, Toyoki Kunitake

研究成果: ジャーナルへの寄稿学術誌査読

79 被引用数 (Scopus)

抄録

Myoglobin (Mb), a water-soluble hemoprotein, is effectively organized together with NADH and FMN coenzymes on the surface of aqueous synthetic bilayer membranes. The redox activity and the binding mode of membrane-bound Mb molecules were studied by UV–visible and ESR spectroscopies and the ultrafiltration binding assay. Mb molecules bound onto a mixed bilayer of ammonium (1) and phosphate (2) amphiphiles can efficiently accept an electron from NADH via FMN and subsequently release its electron catalytically to dioxygen and l,2-naphthoquinone-4-sulfonate. Thus, Mb is converted from an oxygen storage protein to a redox enzyme. ESR examination of a cast film of the aqueous mixture indicates that Mb is bound to the mixed bilayer in a precision comparable to conventional membrane-bound enzymes. Implications of the present methodology were discussed in terms of functional conversion of enzymes and design of novel multienzyme systems.

本文言語英語
ページ(範囲)9625-9630
ページ数6
ジャーナルJournal of the American Chemical Society
113
25
DOI
出版ステータス出版済み - 12月 1 1991

!!!All Science Journal Classification (ASJC) codes

  • 触媒
  • 化学 (全般)
  • 生化学
  • コロイド化学および表面化学

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