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

Itaru Hamachi, Shunsaku Noda, Toyoki Kunitake

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Abstract

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.

Original languageEnglish
Pages (from-to)9625-9630
Number of pages6
JournalJournal of the American Chemical Society
Volume113
Issue number25
DOIs
Publication statusPublished - Dec 1 1991

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All Science Journal Classification (ASJC) codes

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

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