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 |
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ページ(範囲) | 9625-9630 |
ページ数 | 6 |
ジャーナル | Journal of the American Chemical Society |
巻 | 113 |
号 | 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