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Báo cáo khoa học: Kinetic and binding studies with purified recombinant proteins ferredoxin reductase, ferredoxin and cytochrome P450 comprising the morpholine mono-oxygenase from Mycobacteriumsp. strain HE5

Chia sẻ: Nguyen Thang | Ngày: | Loại File: PDF | Số trang:12

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The P450morsystem fromMycobacteriumsp. strain HE5, supposed to cata-lyse the hydroxylation of different N-heterocycles, is composed of three components: ferredoxin reductase (FdRmor), Fe3S4 ferredoxin (Fd mor) and cytochrome P450 (P450mor). In this study, we purified Fdmorand P450mor as recombinant proteins as well as FdRmor, which has been isolated previ-ously. Kinetic investigations of the redox couple FdRmor⁄Fdmorrevealed a 30-fold preference for the NADH-dependent reduction of nitroblue tetrazo-lium (NBT) and an absolute requirement for Fd morin this reaction, com-pared with the NADH-dependent reduction of cytochromec. ...

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Nội dung Text: Báo cáo khoa học: Kinetic and binding studies with purified recombinant proteins ferredoxin reductase, ferredoxin and cytochrome P450 comprising the morpholine mono-oxygenase from Mycobacteriumsp. strain HE5

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