The Role of Cytochrome P‐450 in the Hydroperoxide‐Catalyzed Oxidation of Alcohols by Rat‐Liver Microsomes

作者：Anver D. Rahimtula, Peter James O'Brien · 发表于：European Journal of Biochemistry · 年份：1977 · DOI：10.1111/j.1432-1033.1977.tb11658.x · 被引用次数：28 · 研究领域：Alcohol Consumption and Health Effects、Pharmacogenetics and Drug Metabolism、Eicosanoids and Hypertension Pharmacology

The organic hydroperoxide cumene hydroperoxide is capable of oxidizing ethanol to acetaldehyde in the presence of either catalase, purified cytochrome P-450 or rat liver microsomes. Other hemoproteins like horseradish peroxidase, cytochrome c or hemoglobin were ineffective. In addition to ethanol, higher alcohols like 1-propanol, 1-butanol and 1-pentanol are also oxidized to their corresponding aldehydes to a lesser extent. Other organic hydroxyperoxides will replace cumene hydroperoxide in oxidizing ethanol but less effectively. The cumene-hydroperoxide-dependent ethanol oxidation in microsomes was inhibited partially by cytochrome P-450 inhibitors but was unaffected by catalase inhibitors. Phenobarbital pretreatment of rats increased the specific activity of the cumene-hydroperoxide-dependent ethanol oxidation per mg of microsomes about seven-fold. The evidence suggests that cytochrome P-450 rather than catalase is the enzyme responsible for hydroperoxide-dependent ethanol oxidation. However, when H2O2 is used in place of cumene hydroperoxide, the microsomal ethanol oxidation closely resembles the catalase system.