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Inactivation of the iron-containing superoxide dismutase of escherichia coli by hydrogen peroxide

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:5217384
The iron-containing Fe(SOD) and the copper and zinc-containing (Cu,ZnSOD) superoxide dismutases (SOD) are inactivated by H/sub 2/O/sub 2/; whereas the corresponding manganese-containing enzyme (MnSOD) is resistant to H/sub 2/O/sub 2/. In the case of Cu, ZnSOD, studies of the effects of pH on inactivation demonstrated that HO/sub 2//sup -/ was the damaging species; while amino acid analysis showed that a loss of a single histidine per subunit correlated with loss of activity. The FeSOD from E. coli is inactivated to a limit of 90% by H/sub 2/O/sub 2/. The 10% residual H/sub 2/O/sub 2/-resistant activity differs form the activity of the native enzyme in being more sensitive to thermal inactivation and less sensitive towards inhibition by azide. Inactivation of FeSOD by H/sub 2/O/sub 2/ correlated with (1) loss of tryptophan and of iron, but not of histidine; (2) bleaching of absorption in the visible and alteration of the UV spectrum; and (3) increase in the intrinsic fluorescence due to tryptophan residues. Reversible removal of the iron demonstrated that the 10% H/sub 2/O/sub 2/-resistant activity of FeSOD was not due to some occupancy of the Fe site by manganese. Compounds such as histidine and urate, which protect Cu,ZnSOD against inactivation by H/sub 2/O/sub 2/, did not protect FeSOD.
Research Organization:
Duke Univ., Durham, NC
OSTI ID:
5217384
Report Number(s):
CONF-8606151-
Conference Information:
Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 45:6
Country of Publication:
United States
Language:
English