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 language | English |
|---|---|
| Pages (from-to) | 9625-9630 |
| Number of pages | 6 |
| Journal | Journal of the American Chemical Society |
| Volume | 113 |
| Issue number | 25 |
| DOIs | |
| Publication status | Published - Dec 1 1991 |
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All Science Journal Classification (ASJC) codes
- Catalysis
- Chemistry(all)
- Biochemistry
- Colloid and Surface Chemistry
Cite this
Functional Conversion of Myoglobin Bound to Synthetic Bilayer Membranes : From Dioxygen Storage Protein to Redox Enzyme. / Hamachi, Itaru; Noda, Shunsaku; Kunitake, Toyoki.
In: Journal of the American Chemical Society, Vol. 113, No. 25, 01.12.1991, p. 9625-9630.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Functional Conversion of Myoglobin Bound to Synthetic Bilayer Membranes
T2 - From Dioxygen Storage Protein to Redox Enzyme
AU - Hamachi, Itaru
AU - Noda, Shunsaku
AU - Kunitake, Toyoki
PY - 1991/12/1
Y1 - 1991/12/1
N2 - 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.
AB - 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.
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U2 - 10.1021/ja00025a031
DO - 10.1021/ja00025a031
M3 - Article
VL - 113
SP - 9625
EP - 9630
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 25
ER -