{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T05:16:49Z","timestamp":1779340609814,"version":"3.51.4"},"reference-count":59,"publisher":"American Society for Microbiology","issue":"23","license":[{"start":{"date-parts":[[1995,12,1]],"date-time":"1995-12-01T00:00:00Z","timestamp":817776000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[1995,12]]},"abstract":"<jats:p>The conventional model of oxidative DNA damage posits a role for superoxide (O2-) as a reductant for iron, which subsequently generates a hydroxyl radical by transferring the electron to H2O2. The hydroxyl radical then attacks DNA. Indeed, mutants of Escherichia coli that lack superoxide dismutase (SOD) were 10-fold more vulnerable to DNA oxidation by H2O2 than were wild-type cells. Even the pace of DNA damage by endogenous oxidants was great enough that the SOD mutants could not tolerate air if enzymes that repair oxidative DNA lesions were inactive. However, DNA oxidation proceeds in SOD-proficient cells without the involvement of O2-, as evidenced by the failure of SOD overproduction or anaerobiosis to suppress damage by H2O2. Furthermore, the mechanism by which excess O2- causes damage was called into question when the hypersensitivity of SOD mutants to DNA damage persisted for at least 20 min after O2- had been dispelled through the imposition of anaerobiosis. That behavior contradicted the standard model, which requires that O2- be present to rereduce cellular iron during the period of exposure to H2O2. Evidently, DNA oxidation is driven by a reductant other than O2-, which leaves the mechanism of damage promotion by O2- unsettled. One possibility is that, through its well-established ability to leach iron from iron-sulfur clusters, O2- increases the amount of free iron that is available to catalyze hydroxyl radical production. Experiments with iron transport mutants confirmed that increases in free-iron concentration have the effect of accelerating DNA oxidation. Thus, O2- may be genotoxic only in doses that exceed those found in SOD-proficient cells, and in those limited circumstances it may promote DNA damage by increasing the amount of DNA-bound iron.<\/jats:p>","DOI":"10.1128\/jb.177.23.6782-6790.1995","type":"journal-article","created":{"date-parts":[[2016,11,9]],"date-time":"2016-11-09T15:17:18Z","timestamp":1478704638000},"page":"6782-6790","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":203,"title":["Superoxide and the production of oxidative DNA damage"],"prefix":"10.1128","volume":"177","author":[{"given":"K","family":"Keyer","sequence":"first","affiliation":[{"name":"Department of Microbiology, University of Illinois, Urbana 61801, USA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A S","family":"Gort","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Illinois, Urbana 61801, USA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J A","family":"Imlay","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Illinois, Urbana 61801, USA."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"p_1","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1128\/jb.130.1.187-191.1977","article-title":"Repair of hydrogen peroxide-induced single-strand breaks in Escherichia coli deoxyribonucleic acid","volume":"130","author":"Ananthaswamy H. N.","year":"1977","unstructured":"Ananthaswamy , H. N. , and A. Eisenstark . 1977 . Repair of hydrogen peroxide-induced single-strand breaks in Escherichia coli deoxyribonucleic acid . J. Bacteriol. 130 : 187 - 191 .","journal-title":"J. Bacteriol."},{"key":"p_2","doi-asserted-by":"crossref","first-page":"5471","DOI":"10.1021\/bi00391a039","article-title":"Ferric uptake regulation protein acts as a repressor, employing iron(II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli","volume":"26","author":"Bagg A.","year":"1987","unstructured":"Bagg , A. , and J. B. Neilands . 1987 . Ferric uptake regulation protein acts as a repressor, employing iron(II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli . Biochemistry 26 : 5471 - 5477 .","journal-title":"Biochemistry"},{"key":"p_3","doi-asserted-by":"crossref","first-page":"5214","DOI":"10.1016\/S0021-9258(18)62842-X","article-title":"A mechanism for the production of ethylene from methional. The generation of the hydroxyl radical by xanthine oxidase","volume":"245","author":"Beauchamp C.","year":"1970","unstructured":"Beauchamp , C. , and I. Fridovich . 1970 . A mechanism for the production of ethylene from methional. The generation of the hydroxyl radical by xanthine oxidase . J. Biol. Chem. 245 : 5214 - 5222 .","journal-title":"J. Biol. Chem."},{"key":"p_4","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/0003-2697(71)90370-8","article-title":"Superoxide dismutase: improved assays and an assay applicable to acrylamide gels","volume":"44","author":"Beauchamp C.","year":"1971","unstructured":"Beauchamp , C. , and I. Fridovich . 1971 . Superoxide dismutase: improved assays and an assay applicable to acrylamide gels . Anal. Biochem. 44 : 276 - 287 .","journal-title":"Anal. Biochem."},{"key":"p_5","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/S0021-9258(18)52435-2","article-title":"In vivo competitions between iron and manganese for occupancy of the active site region of the manganesesuperoxide dismutase of Escherichia coli","volume":"266","author":"Beyer W. F.","year":"1991","unstructured":"Beyer , W. F. , Jr. , and I. Fridovich . 1991 . In vivo competitions between iron and manganese for occupancy of the active site region of the manganesesuperoxide dismutase of Escherichia coli . J. Biol. Chem. 266 : 303 - 308 .","journal-title":"J. Biol. Chem."},{"key":"p_6","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1063\/1.555739","article-title":"Reactivity of HO2\/O2\n                  ~ radicals in aqueous solution","volume":"14","author":"Bielski B. H. J.","year":"1985","unstructured":"Bielski , B. H. J. , D. E. Cabelli , and R. L. Arudi . 1985 . Reactivity of HO2\/O2~ radicals in aqueous solution . J. Phys. Chem. Ref. Data 14 : 1041 - 1062 .","journal-title":"J. Phys. Chem. Ref. Data"},{"key":"p_7","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1042\/bj2390169","article-title":"On the superoxide-dependent and independent mechanism of iron mobilization from ferritin by xanthine oxidase. Its implications for oxygen free radical induced tissue destruction during ischemia and inflammation","volume":"239","author":"Biemond P.","year":"1986","unstructured":"Biemond , P. , A. J. G. Swaak , C. M. Beindorff , and J. F. Koster . 1986 . On the superoxide-dependent and independent mechanism of iron mobilization from ferritin by xanthine oxidase. Its implications for oxygen free radical induced tissue destruction during ischemia and inflammation . Biochem. J. 239 : 169 .","journal-title":"Biochem. J."},{"key":"p_8","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/0891-5849(88)90026-3","article-title":"Superoxide dependent iron release from ferritin in inflammatory diseases","volume":"4","author":"Biemond P.","year":"1988","unstructured":"Biemond , P. , A. J. G. Swaak , H. G. van Eijk , and J. F. Koster . 1988 . Superoxide dependent iron release from ferritin in inflammatory diseases . Free Radical Biol. Med. 4 : 185 - 198 .","journal-title":"Free Radical Biol. Med."},{"key":"p_9","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1016\/0006-291X(85)90449-8","article-title":"Is hydroxyl radical generated by the Fenton reaction in vivo","volume":"130","author":"Bilinski T.","year":"1985","unstructured":"Bilinski , T. , Z. Krawiec , A. Liczmanski , and J. Litwinska . 1985 . Is hydroxyl radical generated by the Fenton reaction in vivo ? Biochem. Biophys. Res. Commun. 130 : 533 - 539 .","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"p_10","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1002\/j.1460-2075.1986.tb04256.x","article-title":"Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life","volume":"5","author":"Carlioz A.","year":"1986","unstructured":"Carlioz , A. , and D. Touati . 1986 . Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life ? EMBO J. 5 : 623 - 630 .","journal-title":"EMBO J."},{"key":"p_11","doi-asserted-by":"crossref","first-page":"3189","DOI":"10.1073\/pnas.84.10.3189","article-title":"Endonuclease IV of Escherichia coli is induced by paraquat","volume":"84","author":"Chan E.","year":"1987","unstructured":"Chan , E. , and B. Weiss . 1987 . Endonuclease IV of Escherichia coli is induced by paraquat . Proc. Natl. Acad. Sci. USA 84 : 3189 - 3193 .","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"p_12","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1128\/jb.143.1.529-530.1980","article-title":"Construction of an Hfr strain useful for transferring recA mutations between Escherichia coli strains","volume":"143","author":"Csonka L. N.","year":"1980","unstructured":"Csonka , L. N. , and A. J. Clark . 1980 . Construction of an Hfr strain useful for transferring recA mutations between Escherichia coli strains . J. Bacteriol. 143 : 529 - 530 .","journal-title":"J. Bacteriol."},{"key":"p_13","doi-asserted-by":"crossref","first-page":"1120","DOI":"10.1128\/jb.168.3.1120-1127.1986","article-title":"Endonuclease IV (nfo) mutant of Escherichia coli","volume":"168","author":"Cunningham R. P.","year":"1986","unstructured":"Cunningham , R. P. , S. M. Saporito , S. G. Spitzer , and B. Weiss . 1986 . Endonuclease IV (nfo) mutant of Escherichia coli . J. Bacteriol. 168 : 1120 - 1127 .","journal-title":"J. Bacteriol."},{"key":"p_14","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1146\/annurev.bi.63.070194.004411","article-title":"Repair of oxidative damage to DNA: enzymology and biology. Annu","volume":"61","author":"Demple B.","year":"1994","unstructured":"Demple , B. , and L. Harrison . 1994 . Repair of oxidative damage to DNA: enzymology and biology. Annu . Rev. Biochem. 61 : 915 - 948 .","journal-title":"Rev. Biochem."},{"key":"p_15","doi-asserted-by":"crossref","first-page":"7731","DOI":"10.1073\/pnas.83.20.7731","article-title":"Exonuclease III and endonuclease IV remove 3~ blocks from DNA synthesis primers in H2O2-damaged Escherichia coli","volume":"83","author":"Demple B.","year":"1986","unstructured":"Demple , B. , A. Johnson , and D. Fung . 1986 . Exonuclease III and endonuclease IV remove 3~ blocks from DNA synthesis primers in H2O2-damaged Escherichia coli . Proc. Natl. Acad. Sci. USA 83 : 7731 - 7735 .","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"p_16","doi-asserted-by":"crossref","first-page":"8268","DOI":"10.1073\/pnas.83.21.8268","article-title":"Oxygen-dependent mutagenesis in Escherichia coli lacking superoxide dismutase","volume":"83","author":"Farr S. B.","year":"1986","unstructured":"Farr , S. B. , R. D'Ari , and D. Touati . 1986 . Oxygen-dependent mutagenesis in Escherichia coli lacking superoxide dismutase . Proc. Natl. Acad. Sci. USA 83 : 8268 - 8272 .","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"p_17","doi-asserted-by":"crossref","first-page":"25547","DOI":"10.1016\/S0021-9258(19)74426-3","article-title":"The inactivation of dihydroxyacid dehydratase in Escherichia coli treated with hyperbaric oxygen occurs because of the destruction of its Fe-S cluster, but the enzyme remains in the cell in a form that can be reactivated","volume":"268","author":"Flint D. H.","year":"1993","unstructured":"Flint , D. H. , E. Smyk-Randall , J. F. Tuminello , B. Draczynska-Lusiak , and O. R. Brown . 1993 . The inactivation of dihydroxyacid dehydratase in Escherichia coli treated with hyperbaric oxygen occurs because of the destruction of its Fe-S cluster, but the enzyme remains in the cell in a form that can be reactivated . J. Biol. Chem. 268 : 25547 - 25552 .","journal-title":"J. Biol. Chem."},{"key":"p_18","doi-asserted-by":"crossref","first-page":"22369","DOI":"10.1016\/S0021-9258(18)41538-4","article-title":"The inactivation of Fe-S cluster containing hydro-lyases by superoxide","volume":"268","author":"Flint D. H.","year":"1993","unstructured":"Flint , D. H. , J. F. Tuminello , and M. H. Emptage . 1993 . The inactivation of Fe-S cluster containing hydro-lyases by superoxide . J. Biol. Chem. 268 : 22369 - 22376 .","journal-title":"J. Biol. Chem."},{"key":"p_19","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1126\/science.210504","article-title":"The biology of oxygen radicals","volume":"201","author":"Fridovich I.","year":"1978","unstructured":"Fridovich , I. 1978 . The biology of oxygen radicals . Science 201 : 875 .","journal-title":"Science"},{"key":"p_20","first-page":"19328","article-title":"Superoxide sensitivity of the Escherichia coli aconitase","volume":"266","author":"Gardner P. R.","year":"1991","unstructured":"Gardner , P. R. , and I. Fridovich . 1991 . Superoxide sensitivity of the Escherichia coli aconitase . J. Biol. Sci. 266 : 19328 - 19333 .","journal-title":"J. Biol. Sci."},{"key":"p_21","doi-asserted-by":"crossref","first-page":"6181","DOI":"10.1073\/pnas.87.16.6181","article-title":"Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in E. coli","volume":"87","author":"Greenberg J. T.","year":"1990","unstructured":"Greenberg , J. T. , P. Monach , J. H. Chou , P. D. Josephy , and B. Demple . 1990 . Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in E. coli . Proc. Natl. Acad. Sci. USA 87 : 6181 - 6185 .","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"p_22","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1007\/BF00328074","article-title":"Genetic characterization of the Escherichia coli cyclopropane fatty acid (cfa) locus and neighboring loci","volume":"196","author":"Grogan D. W.","year":"1984","unstructured":"Grogan , D. W. , and J. E. Cronan . 1984 . Genetic characterization of the Escherichia coli cyclopropane fatty acid (cfa) locus and neighboring loci . Mol. Gen. Genet. 196 : 367 - 372 .","journal-title":"Mol. Gen. Genet."},{"key":"p_23","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1007\/BF00269672","article-title":"Regulation of ferric iron transport in Escherichia coli K12: isolation of a constitutive mutant","volume":"182","author":"Hantke K.","year":"1981","unstructured":"Hantke , K. 1981 . Regulation of ferric iron transport in Escherichia coli K12: isolation of a constitutive mutant . Mol. Gen. Genet. 182 : 288 - 292 .","journal-title":"Mol. Gen. Genet."},{"key":"p_24","doi-asserted-by":"crossref","first-page":"3217","DOI":"10.1073\/pnas.89.8.3217","article-title":"Regulatory roles of Fnr, Fur, and Arc in expression of manganese-containing superoxide dismutase in Escherichia coli","volume":"89","author":"Hassan H. M.","year":"1992","unstructured":"Hassan , H. M. , and H. C. H. Sun . 1992 . Regulatory roles of Fnr, Fur, and Arc in expression of manganese-containing superoxide dismutase in Escherichia coli . Proc. Natl. Acad. Sci. USA 89 : 3217 - 3221 .","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"p_25","doi-asserted-by":"crossref","first-page":"29405","DOI":"10.1016\/S0021-9258(18)43893-8","article-title":"Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not","volume":"269","author":"Hausladen A.","year":"1994","unstructured":"Hausladen , A. , and I. Fridovich . 1994 . Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not . J. Biol. Chem. 269 : 29405 - 29408 .","journal-title":"J. Biol. Chem."},{"key":"p_26","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/0022-2836(73)90176-9","article-title":"Genetic analysis of the RecF pathway to genetic recombination in Escherichia coli K-12: isolation and characterization of mutants","volume":"80","author":"Horii Z. I.","year":"1973","unstructured":"Horii , Z. I. , and A. J. Clark . 1973 . Genetic analysis of the RecF pathway to genetic recombination in Escherichia coli K-12: isolation and characterization of mutants . J. Mol. Biol. 80 : 327 - 344 .","journal-title":"J. Mol. Biol."},{"key":"p_27","doi-asserted-by":"crossref","first-page":"985","DOI":"10.1111\/j.1432-1033.1993.tb18457.x","article-title":"Overproduction, purification and characterization of the Escherichia coli ferritin","volume":"218","author":"Hudson S. J.","year":"1993","unstructured":"Hudson , S. J. , S. C. Andrews , C. Hawkins , J. M. Williams , M. Izuhara , F. C. Meldrum , S. Mann , P. M. Harrison , and J. R. Guest . 1993 . Overproduction, purification and characterization of the Escherichia coli ferritin . Eur. J. Biochem. 218 : 985 - 995 .","journal-title":"Eur. J. Biochem."},{"key":"p_28","first-page":"116","article-title":"Chemical changes induced in DNA by ionizing radiation","volume":"32","author":"Hutchinson F.","year":"1985","unstructured":"Hutchinson , F. 1985 . Chemical changes induced in DNA by ionizing radiation . Prog. Nucleic Acid Res. 32 : 116 - 154 .","journal-title":"Prog. Nucleic Acid Res."},{"key":"p_29","first-page":"6957","article-title":"Assay of metabolic superoxide production in Escherichia coli","volume":"266","author":"Imlay J. A.","year":"1991","unstructured":"Imlay , J. A. , and I. Fridovich . 1991 . Assay of metabolic superoxide production in Escherichia coli . J. Biol. Sci. 266 : 6957 - 6965 .","journal-title":"J. Biol. Sci."},{"key":"p_30","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1128\/jb.166.2.519-527.1986","article-title":"Bimodal pattern of killing of DNA-repairdefective or anoxically grown Escherichia coli by hydrogen peroxide","volume":"166","author":"Imlay J. A.","year":"1986","unstructured":"Imlay , J. A. , and S. Linn . 1986 . Bimodal pattern of killing of DNA-repairdefective or anoxically grown Escherichia coli by hydrogen peroxide . J. Bacteriol. 166 : 519 - 527 .","journal-title":"J. Bacteriol."},{"key":"p_31","doi-asserted-by":"crossref","first-page":"2967","DOI":"10.1128\/jb.169.7.2967-2976.1987","article-title":"Mutagenesis and stress responses induced in Escherichia coli by hydrogen peroxide","volume":"169","author":"Imlay J. A.","year":"1987","unstructured":"Imlay , J. A. , and S. Linn . 1987 . Mutagenesis and stress responses induced in Escherichia coli by hydrogen peroxide . J. Bacteriol. 169 : 2967 - 2976 .","journal-title":"J. Bacteriol."},{"key":"p_32","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1126\/science.3287616","article-title":"DNA damage and oxygen radical toxicity","volume":"240","author":"Imlay J. A.","year":"1988","unstructured":"Imlay , J. A. , and S. Linn . 1988 . DNA damage and oxygen radical toxicity . Science 240 : 1302 - 1309 .","journal-title":"Science"},{"key":"p_33","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1126\/science.2834821","article-title":"Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro","volume":"240","author":"Imlay J. A.","year":"1988","unstructured":"Imlay , J. A. , and S. Linn . 1988 . Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro . Science 240 : 640 - 642 .","journal-title":"Science"},{"key":"p_34","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/0921-8734(90)90022-J","article-title":"A methyl viologen-sensitive mutant of the nematode Caenorhabditis elegans","volume":"237","author":"Ishii N.","year":"1990","unstructured":"Ishii , N. , K. Takahashi , S. Tomita , T. Keino , S. Honda , K. Yoshino , and K. Suzuki . 1990 . A methyl viologen-sensitive mutant of the nematode Caenorhabditis elegans . Mutat. Res. 237 : 165 - 171 .","journal-title":"Mutat. Res."},{"key":"p_35","doi-asserted-by":"crossref","first-page":"6212","DOI":"10.1128\/jb.175.19.6212-6219.1993","article-title":"Characterization of the ferrous iron uptake system of Escherichia coli","volume":"175","author":"Kammler M.","year":"1993","unstructured":"Kammler , M. , C. Schon , and K. Hantke . 1993 . Characterization of the ferrous iron uptake system of Escherichia coli . J. Bacteriol. 175 : 6212 - 6219 .","journal-title":"J. Bacteriol."},{"key":"p_36","doi-asserted-by":"crossref","first-page":"2819","DOI":"10.1073\/pnas.77.5.2819","article-title":"DNA-damaging agents stimulate gene expression at specific loci in Escherichia coli","volume":"77","author":"Kenyon C. J.","year":"1980","unstructured":"Kenyon , C. J. , and G. C. Walker . 1980 . DNA-damaging agents stimulate gene expression at specific loci in Escherichia coli . Proc. Natl. Acad. Sci. USA 77 : 2819 - 2823 .","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"p_37","doi-asserted-by":"crossref","first-page":"4724","DOI":"10.1016\/S0021-9258(18)61255-4","article-title":"~,~-Dihydroxyisovalerate dehydratase: a superoxide-sensitive enzyme","volume":"262","author":"Kuo C. F.","year":"1987","unstructured":"Kuo , C. F. , T. Mashino , and I. Fridovich . 1987 . ~,~-Dihydroxyisovalerate dehydratase: a superoxide-sensitive enzyme . J. Biol. Chem. 262 : 4724 - 4727 .","journal-title":"J. Biol. Chem."},{"key":"p_38","doi-asserted-by":"crossref","first-page":"1366","DOI":"10.1073\/pnas.69.6.1366","article-title":"Indirect suppression of recB and recC mutations by exonuclease I deficiency","volume":"69","author":"Kushner S. R.","year":"1972","unstructured":"Kushner , S. R. , H. Nagaishi , and A. J. Clark . 1972 . Indirect suppression of recB and recC mutations by exonuclease I deficiency . Proc. Natl. Acad. Sci. USA 69 : 1366 - 1370 .","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"p_39","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1242\/jcs.1984.Supplement_6.19","article-title":"Toxicity, mutagenesis and stress responses induced in Escherichia coli by hydrogen peroxide","volume":"6","author":"Linn S.","year":"1987","unstructured":"Linn , S. , and J. A. Imlay . 1987 . Toxicity, mutagenesis and stress responses induced in Escherichia coli by hydrogen peroxide . J. Cell Sci. Suppl. 6 : 289 - 301 .","journal-title":"J. Cell Sci. Suppl."},{"key":"p_40","doi-asserted-by":"crossref","first-page":"5892","DOI":"10.1073\/pnas.89.13.5892","article-title":"Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon","volume":"89","author":"Liochev S. I.","year":"1992","unstructured":"Liochev , S. I. , and I. Fridovich . 1992 . Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon . Proc. Natl. Acad. Sci. USA 89 : 5892 - 5896 .","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"p_41","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1128\/jb.157.2.622-626.1984","article-title":"Isolation of catalase-deficient Escherichia coli mutants and genetic mapping of katE, a locus that affects catalase activity","volume":"157","author":"Loewen P. C.","year":"1984","unstructured":"Loewen , P. C. 1984 . Isolation of catalase-deficient Escherichia coli mutants and genetic mapping of katE, a locus that affects catalase activity . J. Bacteriol. 157 : 622 - 626 .","journal-title":"J. Bacteriol."},{"key":"p_42","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/0014-5793(78)80116-1","article-title":"Superoxide-dependent production of hydroxyl radical catalyzed by iron-EDTA complex","volume":"86","author":"McCord J. M.","year":"1978","unstructured":"McCord , J. M. , and E. D. Day , Jr. 1978 . Superoxide-dependent production of hydroxyl radical catalyzed by iron-EDTA complex . FEBS Lett. 86 : 139 - 142 .","journal-title":"FEBS Lett."},{"key":"p_43","first-page":"6049","article-title":"Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)","volume":"244","author":"McCord J. M.","year":"1969","unstructured":"McCord , J. M. , and I. Fridovich . 1969 . Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein) . J. Biol. Chem. 244 : 6049 - 6055 .","journal-title":"J. Biol. Chem."},{"key":"p_44","doi-asserted-by":"crossref","first-page":"1024","DOI":"10.1073\/pnas.68.5.1024","article-title":"An enzyme-based theory of obligate anaerobiosis: the physiological function of superoxide dismutase","volume":"68","author":"McCord J. M.","year":"1971","unstructured":"McCord , J. M. , B. B. Keele , Jr. , and I. Fridovich . 1971 . An enzyme-based theory of obligate anaerobiosis: the physiological function of superoxide dismutase . Proc. Natl. Acad. Sci. USA 68 : 1024 - 1027 .","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"p_45","unstructured":"Miller J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Cold Spring Harbor N.Y."},{"key":"p_46","doi-asserted-by":"crossref","first-page":"886","DOI":"10.1128\/jb.112.2.886-893.1972","article-title":"Dominant mutations (lex) in Escherichia coli K-12 which affect radiation sensitivity and frequency of ultraviolet light-induced mutations","volume":"112","author":"Mount D. M.","year":"1972","unstructured":"Mount , D. M. , K. B. Low , and S. J. Edmiston . 1972 . Dominant mutations (lex) in Escherichia coli K-12 which affect radiation sensitivity and frequency of ultraviolet light-induced mutations . J. Bacteriol. 112 : 886 - 893 .","journal-title":"J. Bacteriol."},{"key":"p_47","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/0891-5849(92)90178-J","article-title":"Selection and analysis of superoxide dismutase mutants of Neurospora","volume":"13","author":"Munkres K. D.","year":"1992","unstructured":"Munkres , K. D. 1992 . Selection and analysis of superoxide dismutase mutants of Neurospora . Free Radical Biol. Med. 13 : 305 - 318 .","journal-title":"Free Radical Biol. Med."},{"key":"p_48","doi-asserted-by":"crossref","first-page":"4928","DOI":"10.1128\/jb.174.15.4928-4934.1992","article-title":"Nucleotide sequence of Streptococcus mutans superoxide dismutase gene and isolation of insertion mutants","volume":"174","author":"Nakayama K.","year":"1992","unstructured":"Nakayama , K. 1992 . Nucleotide sequence of Streptococcus mutans superoxide dismutase gene and isolation of insertion mutants . J. Bacteriol. 174 : 4928 - 4934 .","journal-title":"J. Bacteriol."},{"key":"p_49","doi-asserted-by":"crossref","first-page":"1939","DOI":"10.1128\/jb.176.7.1939-1943.1994","article-title":"Rapid viability loss on exposure to air in a superoxide dismutase-deficient mutant of Porphyromonas gingivalis","volume":"176","author":"Nakayama K.","year":"1994","unstructured":"Nakayama , K. 1994 . Rapid viability loss on exposure to air in a superoxide dismutase-deficient mutant of Porphyromonas gingivalis . J. Bacteriol. 176 : 1939 - 1943 .","journal-title":"J. Bacteriol."},{"key":"p_50","doi-asserted-by":"crossref","first-page":"2761","DOI":"10.1073\/pnas.86.8.2761","article-title":"Null mutation of copper\/zinc superoxide dismutase in Drosophila confers hypersensitivity to paraquat and reduced longevity","volume":"86","author":"Phillips J. P.","year":"1989","unstructured":"Phillips , J. P. , S. D. Campbell , D. Michaud , M. Charbonneau , and A. J. Hilliker . 1989 . Null mutation of copper\/zinc superoxide dismutase in Drosophila confers hypersensitivity to paraquat and reduced longevity . Proc. Natl. Acad. Sci. USA 86 : 2761 - 2765 .","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"p_51","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/0014-5793(82)80214-7","article-title":"Superoxide-dependent formation of hydroxyl radicals from NADH and NADPH in the presence of iron salts","volume":"142","author":"Rowley D. A.","year":"1982","unstructured":"Rowley , D. A. , and B. Halliwell . 1982 . Superoxide-dependent formation of hydroxyl radicals from NADH and NADPH in the presence of iron salts . FEBS Lett. 142 : 39 .","journal-title":"FEBS Lett."},{"key":"p_52","unstructured":"Sambrook J. E. F. Fritsch and T. Maniatis. 1989. Molecular cloning: a laboratory manual 2nd ed. Cold Spring Harbor Laboratory Press Cold Spring Harbor N.Y."},{"key":"p_53","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1007\/BF00339011","article-title":"Molecular cloning of the fnr gene of Escherichia coli K12","volume":"181","author":"Shaw D. J.","year":"1981","unstructured":"Shaw , D. J. , and J. R. Guest . 1981 . Molecular cloning of the fnr gene of Escherichia coli K12 . Mol. Gen. Genet. 181 : 95 - 100 .","journal-title":"Mol. Gen. Genet."},{"key":"p_54","first-page":"531","article-title":"Fur regulon in gramnegative bacteria. Identification and characterization of new iron-regulated Escherichia coli genes by a fur titration assay","volume":"236","author":"Stojiljkovic I.","year":"1994","unstructured":"Stojiljkovic , I. , A. J. Baumler , and K. Hantke . 1994 . Fur regulon in gramnegative bacteria. Identification and characterization of new iron-regulated Escherichia coli genes by a fur titration assay . J. Mol. Biol. 236 : 531 - 545 .","journal-title":"J. Mol. Biol."},{"key":"p_55","doi-asserted-by":"crossref","first-page":"2305","DOI":"10.1128\/jb.177.9.2305-2314.1995","article-title":"Lethal oxidative damage and mutagenesis are generated by iron in ~fur mutants of Escherichia coli: protective role of superoxide dismutase","volume":"177","author":"Touati D.","year":"1995","unstructured":"Touati , D. , M. Jacques , B. Tardat , L. Bouchard , and S. Despied . 1995 . Lethal oxidative damage and mutagenesis are generated by iron in ~fur mutants of Escherichia coli: protective role of superoxide dismutase . J. Bacteriol. 177 : 2305 - 2314 .","journal-title":"J. Bacteriol."},{"key":"p_56","doi-asserted-by":"crossref","first-page":"3820","DOI":"10.1073\/pnas.83.11.3820","article-title":"A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen","volume":"83","author":"van Loon A. P. G. M.","year":"1986","unstructured":"van Loon , A. P. G. M. , B. Pesold-Hurt , and G. Schatz . 1986 . A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen . Proc. Natl. Acad. Sci. USA 83 : 3820 - 3824 .","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"p_57","doi-asserted-by":"crossref","first-page":"1082","DOI":"10.1128\/jb.126.3.1082-1088.1976","article-title":"Genetic mapping of xthA, the structural gene for exonuclease III in E. coli K-12","volume":"126","author":"White B. J.","year":"1976","unstructured":"White , B. J. , S. J. Hochhauser , N. M. Cintron , and B. Weiss . 1976 . Genetic mapping of xthA, the structural gene for exonuclease III in E. coli K-12 . J. Bacteriol. 126 : 1082 - 1088 .","journal-title":"J. Bacteriol."},{"key":"p_58","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1042\/bj1820625","article-title":"Comparison of superoxide with other reducing agents in the biological production of hydroxyl radicals","volume":"182","author":"Winterbourn C. C.","year":"1979","unstructured":"Winterbourn , C. C. 1979 . Comparison of superoxide with other reducing agents in the biological production of hydroxyl radicals . Biochem. J. 182 : 625 - 628 .","journal-title":"Biochem. J."},{"key":"p_59","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1042\/bj1970171","article-title":"The composition and the structure of bacterioferritin of E. coli","volume":"197","author":"Yariv J.","year":"1981","unstructured":"Yariv , J. , A. J. Kalb , R. Sperling , E. R. Bauminger , S. G. Cohen , and S. Ofer . 1981 . The composition and the structure of bacterioferritin of E. coli . Biochem. J. 197 : 171 - 175 .","journal-title":"Biochem. J."}],"container-title":["Journal of Bacteriology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/jb.177.23.6782-6790.1995","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/jb.177.23.6782-6790.1995","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,7,29]],"date-time":"2021-07-29T17:52:59Z","timestamp":1627581179000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/jb.177.23.6782-6790.1995"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1995,12]]},"references-count":59,"journal-issue":{"issue":"23","published-print":{"date-parts":[[1995,12]]}},"alternative-id":["10.1128\/jb.177.23.6782-6790.1995"],"URL":"https:\/\/doi.org\/10.1128\/jb.177.23.6782-6790.1995","relation":{},"ISSN":["0021-9193","1098-5530"],"issn-type":[{"value":"0021-9193","type":"print"},{"value":"1098-5530","type":"electronic"}],"subject":[],"published":{"date-parts":[[1995,12]]},"assertion":[{"value":"2021-01-31","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}