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• W1587799155 abstract "Summary Superoxide ( O 2 − ) is a primary agent of intracellular oxidative stress. Genetic studies in many organisms have confirmed that excess O 2 − disrupts metabolism, but to date only a small family of [4 Fe ‐4 S ] dehydratases have been identified as direct targets. This investigation reveals that in E scherichia coli O 2 − also poisons a broader cohort of non‐redox enzymes that employ ferrous iron atoms as catalytic cofactors. These enzymes were inactivated by O 2 − both in vitro and in vivo . Although the enzymes are known targets of hydrogen peroxide, the outcome with O 2 − differs substantially. When purified enzymes were damaged by O 2 − in vitro , activity could be completely restored by iron addition, indicating that the O 2 − treatment generated an apoprotein without damaging the protein polypeptide. Superoxide stress inside cells caused the progressive mismetallation of these enzymes with zinc, which confers little activity. When O 2 − stress was terminated, cells gradually restored activity by extracting zinc from the proteins. The overloading of cells with zinc caused mismetallation even without O 2 − stress. These results support a model in which O 2 − repeatedly excises iron from these enzymes, allowing zinc to compete with iron for remetallation of their apoprotein forms. This action substantially expands the physiological imprint of O 2 − stress." @default.
• W1587799155 created "2016-06-24" @default.
• W1587799155 creator A5049626416 @default.
• W1587799155 creator A5079628041 @default.
• W1587799155 date "2013-06-07" @default.
• W1587799155 modified "2023-10-03" @default.
• W1587799155 title "Superoxide poisons mononuclear iron enzymes by causing mismetallation" @default.
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• W1587799155 doi "https://doi.org/10.1111/mmi.12263" @default.
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