ABSTRACT
Hydrogen peroxide is generated during aerobic metabolism and is capable of damaging critical biomolecules. However, mutants ofEscherichia coli that are devoid of catalase typically exhibit no adverse phenotypes during growth in aerobic media. We discovered that catalase mutants retain the ability to rapidly scavenge H2O2 whether it is formed internally or provided exogenously. Analysis of candidate genes revealed that the residual activity is due to alkyl hydroperoxide reductase (Ahp). Mutants that lack both Ahp and catalase could not scavenge H2O2. These mutants excreted substantial amounts of H2O2, and they grew poorly in air. Ahp is kinetically a more efficient scavenger of trace H2O2 than is catalase and therefore is likely to be the primary scavenger of endogenous H2O2. Accordingly, mutants that lack Ahp accumulated sufficient hydrogen peroxide to induce the OxyR regulon, whereas the OxyR regulon remained off in catalase mutants. Catalase still has an important role in wild-type cells, because the activity of Ahp is saturated at a low (10−5 M) concentration of H2O2. In contrast, catalase has a high K
m
, and it therefore becomes the predominant scavenger when H2O2 concentrations are high. This arrangement is reasonable because the cell cannot provide enough NADH for Ahp to rapidly degrade large amounts of H2O2. In sum,E. coli does indeed generate substantial H2O2, but damage is averted by the scavenging activity of Ahp.
Mechanistic insights into Escherichia coli alkyl hydroperoxide reductase complex formation
