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• W2068422015 abstract "Cytochrome P450 (P450) 3A4 is the most abundant human P450 and oxidizes a diversity of substrates, including various drugs, steroids, carcinogens, and macrolide natural products. In some reactions, positive cooperativity has been reported in microsomal studies. Flavonoids, e.g., 7,8-benzoflavone (α-naphthoflavone, αNF), have been shown to stimulate some reactions but not others. In systems containing purified recombinant bacterial P450 3A4, positive cooperativity was seen in oxidations of several substrates, including testosterone, 17β-estradiol, amitriptyline, and most notably aflatoxin (AF) B1. With these and other reactions, αNF typically reduced cooperativity (i.e., the n value in a Hill plot) while either stimulating or inhibiting reactions. With the substrate AFB1, αNF both stimulated 8,9-epoxidation and inhibited 3α-hydroxylation. The same patterns were seen with AFB1 in a fused P450 3A4−NADPH-P450 reductase protein. αNF did not alter patterns of activity plotted as a function of NADPH-P450 reductase concentration in systems containing the individual proteins. The patterns of AFB1 oxidation to the two products were modified considerably in systems in which NADPH-P450 reductase was replaced with a flavodoxin or ferredoxin system, iodosylbenzene, or cumene hydroperoxide. AFB2, which differs from AFB1 only in the presence of a saturated 8,9-bond, was not oxidized by P450 3A4 but could inhibit AFB1 oxidation. These and other results are considered in the context of several possible models. The results support a model in which an allosteric site is involved, although the proximity of this putative site to the catalytic site cannot be ascertained as of yet. In order to explain the differential effects of αNF and reduction systems on the two oxidations of AFB1, a model is presented in which binding of substrate in a particular conformation can facilitate oxygen activation to enhance catalysis." @default.
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• W2068422015 date "1997-01-01" @default.
• W2068422015 modified "2023-10-18" @default.
• W2068422015 title "Cooperativity in Oxidations Catalyzed by Cytochrome P450 3A4" @default.
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• W2068422015 doi "https://doi.org/10.1021/bi962359z" @default.
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