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Oxygen toxicity and the superoxide dismutase.
Journal of Bacteriology
|June 1, 1973
Summary
Superoxide dismutase (SOD) protects bacteria like E. coli from oxygen toxicity, while catalase plays a lesser role. SOD induction enhances resistance to hyperbaric oxygen and streptonigrin antibiotic lethality.
Area of Science:
- Microbiology
- Biochemistry
- Cellular Biology
Background:
- Oxygen is essential for aerobic life but can be toxic, generating reactive oxygen species.
- Superoxide radical (O(2)(-)) is a key mediator of oxygen toxicity.
- Enzymatic defenses, such as superoxide dismutase and catalase, protect cells from oxidative damage.
Purpose of the Study:
- To investigate the role of superoxide dismutase and catalase in bacterial defense against oxygen toxicity.
- To determine if superoxide dismutase induction confers resistance to hyperbaric oxygen and antibiotic-induced oxidative stress.
Main Methods:
- Comparing oxygen-induced changes in superoxide dismutase and catalase levels in Escherichia coli B and Bacillus subtilis.
- Assessing the resistance of induced and uninduced bacterial cells to hyperbaric oxygen.
- Evaluating the effect of streptonigrin, an antibiotic that generates superoxide radicals, on bacterial survival under aerobic conditions.
Main Results:
- Oxygen induced superoxide dismutase in E. coli B but not in B. subtilis.
- E. coli B with induced superoxide dismutase showed increased resistance to hyperbaric oxygen.
- B. subtilis catalase was induced by oxygen, while E. coli B catalase was not.
- Induced superoxide dismutase in E. coli B conferred resistance to streptonigrin lethality in the presence of oxygen.
Conclusions:
- Superoxide dismutase is a crucial defense mechanism against oxygen toxicity in bacteria.
- Catalase plays a secondary role in protecting against oxygen toxicity compared to superoxide dismutase.
- The ability to induce superoxide dismutase is important for bacterial survival under high oxygen conditions.