{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,5]],"date-time":"2026-04-05T09:17:08Z","timestamp":1775380628452,"version":"3.50.1"},"reference-count":63,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2011,3,7]],"date-time":"2011-03-07T00:00:00Z","timestamp":1299456000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2011,4]]},"abstract":"<jats:title>Summary<\/jats:title>\n                  <jats:p>\n                    The genome of\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    encodes two class I ribonucleotide reductases. The first, NrdAB, is a well\u2010studied iron\u2010dependent enzyme that is essential for aerobic growth. The second, NrdEF, is not functional under routine conditions, and its role is obscure. Recent studies demonstrated that NrdEF can be activated\n                    <jats:italic>in vitro<\/jats:italic>\n                    by manganese as well as iron. Since iron enzymes are potential targets for hydrogen peroxide, and since the\n                    <jats:italic>nrdHIEF<\/jats:italic>\n                    operon is induced during H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    stress, we hypothesized that H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    might inactivate NrdAB and that NrdEF might be induced to compensate. This idea was tested using\n                    <jats:italic>E. coli<\/jats:italic>\n                    mutants that are chronically stressed by H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    . Contrary to expectation, NrdAB remained active. Its resistance to H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    depended upon YfaE, which helps to activate NrdB. The induction of NrdEF during H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    stress was mediated by the inactivation of Fur, an iron\u2010dependent repressor. This regulatory arrangement implied that NrdEF has a physiological role during periods of iron starvation. Indeed, NrdEF supported cell replication in iron\u2010depleted cells. Iron bound to NrdF when it was expressed in iron\u2010rich cells, but NrdEF was functional only in cells that were both iron\u2010depleted and manganese\u2010rich. Thus NrdEF supports DNA replication when iron is unavailable to activate the housekeeping NrdAB enzyme.\n                  <\/jats:p>","DOI":"10.1111\/j.1365-2958.2011.07593.x","type":"journal-article","created":{"date-parts":[[2011,2,21]],"date-time":"2011-02-21T08:19:20Z","timestamp":1298276360000},"page":"319-334","source":"Crossref","is-referenced-by-count":131,"title":["The alternative aerobic ribonucleotide reductase of\n                    <i>Escherichia coli<\/i>\n                    , NrdEF, is a manganese\u2010dependent enzyme that enables cell replication during periods of iron starvation"],"prefix":"10.1111","volume":"80","author":[{"given":"Julia E.","family":"Martin","sequence":"first","affiliation":[]},{"given":"James A.","family":"Imlay","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2011,3,7]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1080\/10715760903140568"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2009.06699.x"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.96.11.6161"},{"key":"e_1_2_6_5_1","doi-asserted-by":"crossref","first-page":"20682","DOI":"10.1016\/S0021-9258(19)36739-0","article-title":"Substitution of manganese for iron in ribonucleotide reductase from Escherichia coli. 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