| Literature DB >> 6422989 |
R Bernhardt, A Makower, G R Jänig, K Ruckpaul.
Abstract
Fluorescein isothiocyanate (FITC) has been selectively bound to the epsilon-amino group of lysine-382 in cytochrome P-450 LM2 (RH, reduced-flavoprotein: oxygen oxidoreductase (RH-hydroxylating), EC 1.14.14.1) at pH 8.15. Benzphetamine N-demethylase activity of the reconstituted FITC-modified cytochrome P-450 LM2 was inhibited by 25%. This inhibition has been shown to be due to an impaired electron transfer from the NADPH-cytochrome P-450 reductase (NADPH: ferricytochrome oxidoreductase, EC 1.6.2.4) to the haemoprotein. The data indicate that cytochrome P-450 interacts with the flavoprotein via electrostatic interactions.Entities:
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Year: 1984 PMID: 6422989 DOI: 10.1016/0167-4838(84)90143-2
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002