Nitrite binding to cytochrome P-450 from liver microsomes of trout (Salmo gairdneri Rich.) and effects on two microsomal enzymes.
Addition of nitrite to dithionite-reduced trout liver microsomes leads to the conversion of cytochrome P-450 into a cytochrome P-420-NO complex, as it does in mammalian microsomes. A loss in cytochrome P-450 and an inhibition of aminopyrine demethylase (AP) activity were observed in vitro at nitrite-concentrations found in the liver of trout exposed in vivo to this toxin. Nitrite had no effect on dimethylaniline monooxygenase (DMA), a cytochrome P-450-independent enzyme.
D000633:Aminopyrine N-Demethylase / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D066298:In Vitro Techniques; D008862:Microsomes, Liver / Q000187:drug effects / Q000201:enzymology*; D009573:Nitrites / Q000378:metabolism* / Q000633:toxicity*; D010105:Oxygenases / Q000378:metabolism; D011485:Protein Binding; D014337:Trout
D009573:Nitrites; D003577:Cytochrome P-450 Enzyme System; D010105:Oxygenases; C020066:dimethylaniline monooxygenase (N-oxide forming); D000633:Aminopyrine N-Demethylase