Peroxidatic oxidation of benzo[a]pyrene and prostaglandin biosynthesis.
The arachidonic acid dependent oxidation of benzo[a]pyrene to a mixture of 3,6-, 1,6-, and 6,12-quinones has been studied by using enzyme preparations from sheep seminal vesicles. Maximal oxidation is observed at 100 microM benzo[a]pyrene and 150 microM arachidonic acid. The arachidonic acid dependent oxidation is peroxidatic and utilizes prostaglandin G2 (PGG2), generated in situ from arachidonate, as the hydroperoxide substrate. 15-Hydroperoxy-5,8,11,13-eicosatetraenoic acid is equivalent to PGG2 as a hydroperoxide substrate, but hydrogen peroxide, cumene hydroperoxide, and tert-butyl hydroperoxide are much poorer substrates. Arachidonic acid dependent benzo[a]pyrene oxidation by microsomal and solubilized enzyme preparations is markedly.
D000818:Animals; D001580:Benzopyrenes / Q000378:metabolism*; D006418:Heme / Q000378:metabolism; D066298:In Vitro Techniques; D008297:Male; D008706:Methemoglobin / Q000378:metabolism; D008861:Microsomes / Q000201:enzymology; D008862:Microsomes, Liver / Q000378:metabolism; D010084:Oxidation-Reduction; D010545:Peroxides / Q000378:metabolism*; D011451:Prostaglandin-Endoperoxide Synthases / Q000378:metabolism; D011453:Prostaglandins / Q000096:biosynthesis*; D012343:RNA, Transfer / Q000378:metabolism; D051381:Rats; D012669:Seminal Vesicles / Q000648:ultrastructure; D012756:Sheep
D001580:Benzopyrenes; D010545:Peroxides; D011453:Prostaglandins; D006418:Heme; D008706:Methemoglobin; D012343:RNA, Transfer; D011451:Prostaglandin-Endoperoxide Synthases