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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1987-12-16
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pubmed:abstractText |
DT-diaphorase catalyzes the two-electron reduction of the unsubstituted quinone epoxide, 2,3-epoxy-p-benzoquinone, at expense of NAD(P)H with formation of 2-OH-p-benzohydroquinone as the reaction product. The further conversion reactions of 2-OH-p-benzohydroquinone are influenced by the presence of O2 in the medium. Under aerobic conditions, 2-OH-p-benzohydroquinone undergoes autoxidation--probably with formation of 2-OH-semiquinone intermediates--to 2-OH-p-benzoquinone. The latter product is rapidly reduced by DT-diaphorase and, thus, its accumulation can be only observed upon exhaustion of NADPH. Under anaerobic conditions, 2-OH-p-benzohydroquinone does not undergo autoxidation and its accumulation is stoichiometrically (1:1) related to the amount of NADPH oxidized and epoxide substrate reduced. DT-diaphorase also catalyzes the reduction of the disubstituted quinone epoxide, 2,3-dimethyl-2,3-epoxy-1,4-naphthoquinone. Neither the aliphatic epoxide, trans-stilbene oxide, nor the aromatic epoxide, 4,5-epoxy-benzo[a]pyrene are substrates for DT-diaphorase. The reduction of 2,3-epoxy-p-benzoquinone is also catalyzed by the one-electron transfer enzyme, NADPH-cytochrome P450 reductase at a rate similar to that found with DT-diaphorase. However, this reaction differs from that catalyzed by DT-diaphorase in the distribution of molecular products as well as in the relative contribution of nonenzymatic reactions, i.e. semiquinone disproportionation and autoxidation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2,3-epoxy-1,4-benzoquinone,
http://linkedlifedata.com/resource/pubmed/chemical/2-hydroxy-1,4-benzoquinone,
http://linkedlifedata.com/resource/pubmed/chemical/Benzoquinones,
http://linkedlifedata.com/resource/pubmed/chemical/NADP,
http://linkedlifedata.com/resource/pubmed/chemical/NADPH-Ferrihemoprotein Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Quinone Reductases,
http://linkedlifedata.com/resource/pubmed/chemical/Quinones
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pubmed:status |
MEDLINE
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pubmed:issn |
0891-5849
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
181-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3117624-Animals,
pubmed-meshheading:3117624-Benzoquinones,
pubmed-meshheading:3117624-Chromatography, High Pressure Liquid,
pubmed-meshheading:3117624-Electrons,
pubmed-meshheading:3117624-Kinetics,
pubmed-meshheading:3117624-Liver,
pubmed-meshheading:3117624-NADP,
pubmed-meshheading:3117624-NADPH-Ferrihemoprotein Reductase,
pubmed-meshheading:3117624-Oxidation-Reduction,
pubmed-meshheading:3117624-Oxygen Consumption,
pubmed-meshheading:3117624-Quinone Reductases,
pubmed-meshheading:3117624-Quinones,
pubmed-meshheading:3117624-Rats
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pubmed:year |
1987
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pubmed:articleTitle |
DT-diaphorase-catalyzed two-electron reduction of quinone epoxides.
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pubmed:affiliation |
Department of Pathology II, Linköping University, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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