Anion protection of CuZnSOD during peroxidative activity with H2O2

被引:11
作者
Jewett, SL [1 ]
Olmsted, HK [1 ]
Marach, JA [1 ]
Rojas, F [1 ]
Silva, K [1 ]
机构
[1] Calif State Univ Northridge, Dept Chem, Northridge, CA 91330 USA
关键词
superoxide dismutase; hydrogen peroxide; oxidation; copper(I); 8-oxo-histidine; peptide fragmentation; carbonate radical; peroxidase activity; anion; bicarbonate ion; nitrite ion; nitrotyrosine;
D O I
10.1006/bbrc.2000.3092
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The "peroxidase" activity of the copper-zinc superoxide dismutase is a poorly sustained activity because of the competing inactivation of the enzyme. New evidence suggests that the bound oxidant may be partitioning between oxidizing the enzyme or oxidizing small anions, At constant peroxide, nitrite and azide only partially protect the enzyme (50%) against loss of copper(I) and inactivation up to one anion per copper. Beyond that level, there is no further protection. Bicarbonate ion also protects, but: larger amounts are required. These data suggest that there is significant oxidation of the enzyme even in the presence of the small anions and therefore the formation of the bound oxidant cannot be sustained in a true catalytic process. (C) 2000 Academic Press.
引用
收藏
页码:57 / 60
页数:4
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