FEBS Letters · 1999 · 38 citations · 28 references
Life SciencesBiochemistryCellular MetabolismMetabolismRedox BiochemistryCytochrome P450 EnzymesCytochrome P450-mediated MetabolismOxidative MetabolismReactive Oxygen SpeciesRedox MetabolismAscorbate MetabolismCytochrome P450 InhibitionCytochrome P450-mediated OxidationElectron TransferEndoplasmic Reticulum Redox MetabolismProtein Oxidation-reductionProtein Thiol OxidationProtein Thiol Redox State
Addition of, or gulonolactone oxidase-dependent in situ generation of, ascorbate provoked the oxidation of protein thiols, which was accompanied by ascorbate consumption in liver microsomal vesicles. The maximal rate of protein thiol oxidation was similar upon gulonolactone, ascorbate or dehydroascorbate addition. Cytochrome P450 inhibitors (econazole, proadifen, quercetin) decreased ascorbate consumption and the gulonolactone or ascorbate-stimulated thiol oxidation. The results demonstrate that the ascorbate/dehydroascorbate redox couple plays an important role in electron transfer from protein thiols to oxygen in the hepatic endoplasmic reticulum, even in gulonolactone oxidase deficient species.
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