Dual effects of superoxide dismutase on the autoxidation of 1,4-naphthohydroquinone.
The autoxidation of 1,4-naphthohydroquinone, in a phosphate, EDTA buffer at pH 7.4, exhibits an autocatalysis whose lag phase becomes more pronounced in the presence of either the Cu,Zn- or the Mn-containing superoxide dismutases. In contrast, the autoxidation of a second aliquot of the hydroquinone, added after complete oxidation of the first, is linear and is accelerated by superoxide dismutase. Catalase or inactive superoxide dismutase were without effect in either situation. These results are explicable in terms of a free radical chain reaction which is initially propagated by O2- and then, as the quinone accumulates, by univalent reduction of the quinone by the hydroquinone. Reduction of the quinone by O2- diminishes the overall rate of oxidation. It is not necessary to postulate catalysis by superoxide dismutase of the reduction of the semiquinone by O2-.
Ishii
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T
Department of Biochemistry, Duke University Medical Center, Durham, NC 27710.
Fridovich
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I
D000818:Animals; D002417:Cattle; D005609:Free Radicals; D006873:Hydroquinones / Q000378:metabolism*; D007700:Kinetics; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism; D013482:Superoxide Dismutase / Q000378:metabolism*
D005609:Free Radicals; D006873:Hydroquinones; C063601:1,4-naphthohydroquinone; D013482:Superoxide Dismutase; D010100:Oxygen