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- W2053536319 abstract "Rat liver microsomes incubated in the presence of NADPH catalyze the oxidation of menadione (2-methyl-1,4-naphthoquinone) by two pathways: NADPH-cytochrome P-450 reductase and DT-diaphorase. The former pathway gives rise to labile semiquinones which are readily autooxidized as revealed by a nonstoichiometric NADPH oxidation and a concomitant O2 consumption. The reduction of menadione catalyzed by DT-diaphorase on the other hand results in a relatively stable hydroquinone accompanied by a stoichiometric oxidation of NADPH and no O2 consumption. The total amount of NADPH oxidized by a given amount of menadione reflects the relative contributions of the two pathways which can be demonstrated by the addition of selective inhibitors of the two enzymes or by treatment of the rats with phenobarbital or 3-methylcholanthrene which preferentially induces NADPH-cytochrome P-450 reductase and DT-diaphorase, respectively. Addition of cytosol, which contains the bulk of cellular DT-diaphorase, minimizes the formation of semiquinones and the concomitant O2 consumption. Data relating to other quinones are also presented. The results support the earlier proposal that DT-diaphorase serves as a cellular control device against quinone toxicity." @default.
- W2053536319 created "2016-06-24" @default.
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- W2053536319 date "1982-06-01" @default.
- W2053536319 modified "2023-10-14" @default.
- W2053536319 title "DT-diaphorase as a quinone reductase: A cellular control device against semiquinone and superoxide radical formation" @default.
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- W2053536319 doi "https://doi.org/10.1016/0003-9861(82)90202-8" @default.
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