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- W1999922186 abstract "The possible role of cytochrome b5 (cyt b5) in NADPH-dependent microsomal N-demethylations has been studied in a system reconstituted from cytochrome P-450 (cyt P-450), NADPH-cytochrome c reductase, and sodium cholate. Although the amount of formaldehyde formed from benzphetamine or N,N-dimethylaniline in this system was considerably less than that of NADPH oxidized, this stoichiometry became close to 1:1 on addition of cyt b5. When both cyt b5 and NADH-cyt b5 reductase were included in the system, the second of two electrons required for the overall activity could be supplied from NADH, though NADPH and NADPH-cytochrome c reductase were obligatorily required for the supply of the first electron to cyt P-450. It is suggested that, at least in the reconstituted system, cyt b5 can play two roles, i.e. a) improvement of coupling of NADPH oxidation to demethylation, and b) supply of the second electron to cyt P-450." @default.
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- W1999922186 date "1977-03-01" @default.
- W1999922186 modified "2023-09-23" @default.
- W1999922186 title "The roles of cytochrome b5 in a reconstituted N-demethylase system containing cytochrome P-450" @default.
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- W1999922186 doi "https://doi.org/10.1016/0006-291x(77)91059-2" @default.
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