Peroxidative activity of human Cu,Zn-superoxide dismutase.
In addition to the usual superoxide dismutation activity, Cu,Zn-superoxide dismutase (SOD) has a peroxidative function that utilizes its own dismutation product, H2O2 as a substrate. The peroxidative activity of human Cu,Zn-SOD was studied by using a chromogen, 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulfonate) (ABTS) which reacts with OH radicals to form ABTS+. The optimal pH for the peroxidative activity of human Cu,Zn-SOD was 7.6-9.5. The peroxidative activity retained about 50% of the maximum activity when exposed at 40 degrees C for 5 min. The peroxidative activity showed a typical Michaelis-Menten kinetics for ABTS and H2O2 whose K(m) values were 16 microM and 9.3 mM, respectively. The peroxidative activity of human Cu,Zn-SOD was inhibited about 60% by the copper chelator, diethyldithiocarbamate (DDC) at 10 microM while the dismutation activity was not inhibited under a similar condition. We found that there are differences in the effects of temperature and DDC on the dismutation and peroxidative activities of human Cu,Zn-SOD. These results suggest that the amino acid residues which affect the activities of this enzyme may be different between dismutation and peroxidation.
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