DDT-dehydrochlorinase. III. Enzymic oxidation of glutathione☆
Review articleOpen access
1974/01/01 Full-length article DOI: 10.1016/0020-711X(74)90034-2
Journal: International Journal of Biochemistry
Abstract1.1. Highly purified DDT-dehydrpchlorinase (E.G. 126.96.36.199) from DDT-resistant houseflies is able to act as a glutathione coddase. Both the monomeric and tetrameric forms of the enzyme show oxidation activity, which is lost by titration of the DDT-dehydrochlorinase's thirty-two sulphydryl groups with PCMB.2.2. Conditions under which DDT-dehydrochlorinase undergoes glutathione oxidation are studied and compared with those of the ODT-dehydrochlorination activity of the enzyme.3.3. Of the compounds tested for the oxidation activity, only reduced glutathione and thioglycolic acid are substrates, the initial rate of oxidation of the latter being approximately three times that of GSH.4.4. The oxidation-reduction reaction does not involve liberation of protons in the presence of NAD or NADP. The transfer of the hydrogen atoms of the substrate and their subsequent oxidation to water is measured by oxygen consumption. The mechanism via O2- free-radical anions is postulated.
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