Role of Nad(P)h: quinone oxidoreductase in the regulation of intracellular redox state.
This paper is a brief overview of current knowledge about DT-diaphorase [NAD(P)H: Quinone Oxidoreductase, NQO], flavoprotein that catalyzes the obligatory two-electron reduction of a wide variety of substrates. The most efficient substrates are quinones but the enzyme will also reduce quinone-imines, nitro and azo compounds. NQO is unique among known NAD(P)H-oxidizing flavoproteins in being a 2-electron transferring quinone reductase, and play a major role in preventing one-electron reduction of exogenous quinones by other enzymes to auto-oxidable semiquinones and concomitant superoxide-radical generation. Induction of NQO by a variety of xenobiotics (potential sources of free-radical formation which lead to DNA and cell damage) provides protection from the cytotoxic and carcinogenic effects of these compounds. NQO has an important role in the bioreductive activation of various quinones used in cancer chemotherapy.
Mohora
M
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Department of Biochemistry, Carol Davila University of Medicine and Pharmacy, 8 Eroilor Sanitari Str., 76243 Bucharest, Romania.
D000818:Animals; D015870:Gene Expression; D006801:Humans; D008658:Inactivation, Metabolic; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000235:genetics / Q000378:metabolism / Q000493:pharmacokinetics / Q000494:pharmacology*; D010084:Oxidation-Reduction / Q000187:drug effects; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D016660:NAD(P)H Dehydrogenase (Quinone)