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KMID : 0380219990320040321
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Journal of Biochemistry and Molecular Biology
1999 Volume.32 No. 4 p.321 ~ p.325
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Reduction of Nitrosoarene by Purified NAD(P)H-Quinone Oxidoreductase
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Kim Kyung-Soon
Suk Hee-Won
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Abstract
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NAD(P)H-quinone oxidoreductase (EC 1. 6. 99. 2) was purified form S. cerevisiae. The enzyme readily reduced 2,6-dichlorophenolindophenol, a quinonoid redox dye, as well as substituted benzo- and naphthoquinones, and could accept electrons from either NADH or NADPH. The purified NAD(P)H-quinone oxidoreductase turned out to be capable of reducing nitrosoarenes as well as a variety of quinones. A chemical-trapping technique using 4-chloro-1-naphthol was used to show that the N,N-dimethyl-p-benzoquinonediiminium cation was produced in the reduction of 4-nitroso-N,N-dimethylaniline catalyzed by NAD(P)H-quinone oxidoreductase.
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KEYWORD
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NAD(P)H-quinone oxidoreductase, Nitrosoarene
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