Escherichia coli Δfur mutant displays low HPII catalase activity in stationary phase

Abstract

Iron is among the most important micronutrients used by bacteria. As a partner of the Fenton reaction, however, iron potentiates oxygen toxicity. Strict regulation of iron metabolism, and its coupling with regulation of defenses against oxidative stress, is an essential factor for life in the presence of oxygen. In Escherichia coli, iron metabolism is regulated by the Fur protein. A Fur-deficient mutant, in stationary phase, displayed about 30y-fold lower HPII activity than the respective, Fur-proficient parental strain. Deletion of fur seems to affect HPII catalase specifically, since the mutant was capable of inducing HPI catalase when challenged with H₂O₂. Low HPII catalase activity appears to be among the reasons for hydrogen peroxide hypersensitivity of the Δfur mutant.