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Transcriptomic analysis showed that during protracted low\u2010grade <jats:styled-content style=\"fixed-case\"><jats:roman>H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub><\/jats:roman><\/jats:styled-content> stress, <jats:styled-content style=\"fixed-case\"><jats:italic>E<\/jats:italic><\/jats:styled-content><jats:italic>scherichia coli<\/jats:italic> responds by activating both the <jats:styled-content style=\"fixed-case\">OxyR<\/jats:styled-content> defensive regulon and the Fur iron\u2010starvation response. <jats:styled-content style=\"fixed-case\">OxyR<\/jats:styled-content> induced synthesis of two members of the nine\u2010step heme biosynthetic pathway: ferrochelatase (<jats:styled-content style=\"fixed-case\">HemH<\/jats:styled-content>) and an isozyme of coproporphyrinogen <jats:styled-content style=\"fixed-case\">III<\/jats:styled-content> oxidase (<jats:styled-content style=\"fixed-case\">HemF<\/jats:styled-content>). Mutations that blocked either adaptation caused the accumulation of porphyrin intermediates, inadequate activation of heme enzymes, low catalase activity, defective clearance of <jats:styled-content style=\"fixed-case\"><jats:roman>H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub><\/jats:roman><\/jats:styled-content> and a failure to grow. Genetic analysis indicated that <jats:styled-content style=\"fixed-case\">HemH<\/jats:styled-content> induction is needed to compensate for iron sequestration by the mini\u2010ferritin <jats:styled-content style=\"fixed-case\">D<\/jats:styled-content>ps. Dps activity protects <jats:styled-content style=\"fixed-case\">DNA<\/jats:styled-content> and proteins by limiting Fenton chemistry, but it interferes with the ability of <jats:styled-content style=\"fixed-case\">HemH<\/jats:styled-content> to acquire the iron that it needs to complete heme synthesis. <jats:styled-content style=\"fixed-case\">HemF<\/jats:styled-content> is a manganoprotein that displaces <jats:styled-content style=\"fixed-case\">HemN<\/jats:styled-content>, an iron\u2013sulfur enzyme whose synthesis and\/or stability is apparently problematic during <jats:styled-content style=\"fixed-case\"><jats:roman>H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub><\/jats:roman><\/jats:styled-content> stress. Thus, the primary responses to <jats:styled-content style=\"fixed-case\"><jats:roman>H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub><\/jats:roman><\/jats:styled-content>, including the sequestration of iron, require compensatory adjustments in the mechanisms of iron\u2010cofactor synthesis. The results support the growing evidence that oxidative stress is primarily an iron pathology.<\/jats:p>","DOI":"10.1111\/mmi.12967","type":"journal-article","created":{"date-parts":[[2015,2,9]],"date-time":"2015-02-09T08:24:42Z","timestamp":1423470282000},"page":"744-763","source":"Crossref","is-referenced-by-count":67,"title":["The induction of two biosynthetic enzymes helps <scp><i>E<\/i><\/scp><i>scherichia coli<\/i> sustain heme synthesis and activate catalase during hydrogen peroxide stress"],"prefix":"10.1111","volume":"96","author":[{"given":"Stefano","family":"Mancini","sequence":"first","affiliation":[{"name":"Department of Microbiology University of Illinois  Urbana IL 61801 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James A.","family":"Imlay","sequence":"additional","affiliation":[{"name":"Department of Microbiology University of Illinois  Urbana IL 61801 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