The relative induction of mixed-function oxidase specific activity to C-H and C-C1 bond strengths in polychlorinated derivatives of dibenzo-p-dioxin (PCDDs).
The structure-activity relationships between the mixed-function oxidase (MFO) system and six polychlorinated derivatives of dibenzo-p-dioxin (PCDDs) were studied using Sprague Dawley rats. The study was set up in accordance with previous work in these laboratories involving monocyclic hydrocarbons. Three possible mechanisms at the MFO active site are proposed. C-H bond hydroxylation in low chlorine substituted PCDDs, and probable expoxidation in the intermediate chlorinated species including 2378 tetrachlorodibenzodioxin. Benzo[a]pyrene activity induced by some PCDDs appears irrelevant to the desired metabolic result.
D000818:Animals; D001564:Benzo(a)pyrene / Q000494:pharmacology; D001835:Body Weight; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004147:Dioxins / Q000494:pharmacology*; D004790:Enzyme Induction / Q000187:drug effects; D008099:Liver / Q000201:enzymology; D006899:Mixed Function Oxygenases / Q000096:biosynthesis*; D009249:NADP / Q000378:metabolism; D000072317:Polychlorinated Dibenzodioxins / Q000031:analogs & derivatives / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D004147:Dioxins; D000072317:Polychlorinated Dibenzodioxins; D001564:Benzo(a)pyrene; C018073:hexachlorodibenzo-4-dioxin; D009249:NADP; D006899:Mixed Function Oxygenases