Covalent binding of carbon tetrachloride metabolites to the heme moiety of cytochrome P-450 and its degradation products.
Trichloromethyl free radicals (. CCI) produced during a benzoyl peroxide decomposition of CCl4 covalently bind to hemin. Enzymatically produced . CCl3 by an NADPH anaerobic liver microsomal activation of CCl4, covalently binds to heme and heme degradation products from CO-binding particles. 14C from CCl4 covalently binds to heme and heme degradation products from liver CL-binding particles from rats treated with 14CCl4. In vivo covalent binding of 14CCl4 reactive metabolites to proteins from CO-binding particles is higher than that to the whole microsomal proteins. The possible correlation between binding of . CCl3 to heme and protein moieties of P-450 and CCl4 induced P-450 destruction is discussed.
D000818:Animals; D002248:Carbon Monoxide / Q000378:metabolism; D002251:Carbon Tetrachloride / Q000378:metabolism*; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D005609:Free Radicals; D006418:Heme / Q000378:metabolism*; D008054:Lipid Peroxides / Q000378:metabolism; D008297:Male; D008862:Microsomes, Liver / Q000378:metabolism; D011485:Protein Binding; D011524:Protoporphyrins / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains
D005609:Free Radicals; D008054:Lipid Peroxides; D011524:Protoporphyrins; D006418:Heme; D002248:Carbon Monoxide; D003577:Cytochrome P-450 Enzyme System; D002251:Carbon Tetrachloride