title: Polycyclic aromatic hydrocarbon quinone-mediated oxidation reduction cycling catalyzed by a human placental NADPH-linked carbonyl reductase.
abstract: Polycyclic aromatic hydrocarbon quinones, hydroquinones, and glutathionyl adducts of quinones undergo oxidation-reduction (redox) cycling in the presence of NADPH and the NADPH-linked human placental carbonyl reductase. K-region and non-K-region o-quinones and their glutathione adducts are the best substrates of this enzyme; they are reduced to hydroquinones. Under aerobic conditions, the hydroquinones are autoxidized with the formation of potentially hazardous semiquinones and the superoxide anion. Because of these reactions it is unlikely that polycyclic aromatic hydrocarbon quinones or their glutathione adducts are inert products of detoxication in tissues that contain the carbonyl reductase or another enzyme with similar substrate specificity. If superoxide dismutase is added to reaction mixtures containing the carbonyl reductase and quinones, it inhibits redox cycling. Presumably this results from destruction of the superoxide anion which acts as a chain propagator in these reactions.
authors.affiliation: Department of Medicine, University of Chicago, Illinois 60637.
authors.forename: J
authors.initials: J
authors.lastname: Jarabak
mesh_terms: D000429:Alcohol Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D000449:Aldehyde Reductase; D000074408:Aldo-Keto Reductases; D003574:Cytochrome c Group / Q000378:metabolism; D006801:Humans; D006861:Hydrogen Peroxide / Q000378:metabolism; D006873:Hydroquinones / Q000378:metabolism; D010084:Oxidation-Reduction; D010920:Placenta / Q000201:enzymology*; D011809:Quinones / Q000494:pharmacology*; D015219:Substrate Cycling; D013482:Superoxide Dismutase / Q000378:metabolism
chemical_list: D003574:Cytochrome c Group; D006873:Hydroquinones; D011809:Quinones; D006861:Hydrogen Peroxide; D000429:Alcohol Oxidoreductases; D000074408:Aldo-Keto Reductases; D000449:Aldehyde Reductase; D013482:Superoxide Dismutase