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- W1353142 abstract "Publisher Summary This chapter presents studies on FMN-depleted and reconstituted NADPH-cytochrome c (P-450) reductase. Preferential removal of FMN from the hepatic flavoprotein NADPH-cytochrome c (P-450) reductase and reconstitution with FMN and 1-and 5-deazaflavin analogs has permitted an investigation of the role of the two flavins on the enzyme toward various electron acceptors. The enzyme (EC 1.6.2.4) contains one mole each of FAD and FMN per mole protein and functions physiologically in the transfer of electrons from NADPH to cytochrome P-450 in the oxidative metabolism of many substrates. Distinct roles for the flavins during catalysis are proposed and supported by spectrophotometric and potentiometric data, which indicate that FAD and FMN have different oxidation–reduction properties. The studies presented in this chapter were conducted to elucidate the role of the two flavins using purified pig liver reductase and to compare the physicochemical and catalytic properties of FMN-depleted and the reconstituted enzymes to those of holoenzyme. The results show that FMN can be removed and reconstituted on the steapsin- or detergent-solubilized NADPH-cytochrome c (P-450) reductase with restoration of chemical, physical, and catalytic properties." @default.
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- W1353142 date "1980-01-01" @default.
- W1353142 modified "2023-09-26" @default.
- W1353142 title "STUDIES ON FMN-DEPLETED AND RECONSTITUTED NADPH-CYTOCHROME (P-450) REDUCTASE" @default.
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- W1353142 doi "https://doi.org/10.1016/b978-0-12-187701-9.50053-x" @default.
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