1887

Abstract

Catalase (KatA) is known to play an important role in oxidative stress resistance in many bacterial species and a homologue exists in , a member of the enterohepatic species. Here, a mutant was constructed by insertional mutagenesis and its oxidative stress phenotype was investigated. Catalase activity was readily detected [196 units (mg protein crude cell extract)] in the wild-type, whereas the mutant strain was deficient in, but not devoid of, activity. In contrast, strains lack detectable catalase activity and wild-type generally contains higher specific activity than . Wild-type cells tolerated 6 % O for growth, whilst the mutant could not survive at this oxygen level. Even at the optimal O level, the growth of the strain was severely inhibited, which is also in contrast to strains. Wild-type cells withstood exposure to 100 mM HO but the mutant cells were killed by the same treatment. Wild-type cells suffered no significant DNA damage by HO treatment (100 mM for 6 min), whilst the same treatment resulted in severe DNA fragmentation in the mutant. Thus KatA plays an important role as an antioxidant protein.

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2007-04-01
2020-07-11
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