Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli
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Summary: Very little manganese is imported into Escherichia coli under routine growth conditions: the import system is weakly expressed, the manganese content is low, and a manganese‐dependent enzyme is not correctly metallated. Mutants that lack MntH, the importer, grow at wild‐type rates, indicating that manganese plays no critical role. However, MntH supports the growth of iron‐deficient cells, suggesting that manganese can substitute for iron in activating at least some metalloenzymes. MntH is also strongly induced when cells are stressed by hydrogen peroxide. This adaptation is essential, as E. coli cannot tolerate peroxide stress if mntH is deleted. Other workers have observed that manganese improves the ability of a variety of microbes to tolerate oxidative stress, and the prevailing hypothesis is that manganese does so by chemically scavenging hydrogen peroxide and/or superoxide. We found that manganese does not protect peroxide‐stressed cells by scavenging peroxide. Instead, the beneficial effects of manganese correlate with its ability to metallate mononuclear enzymes. Because iron‐loaded enzymes are vulnerable to the Fenton reaction, the substitution of manganese may prevent protein damage. Accordingly, during H 2 O 2 stress, mutants that cannot import manganese and/or are unable to sequester iron suffer high rates of protein oxidation.
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E. coli is iron-centric and Mn2+ import is specifically induced as a response to oxidative stress.
“E. coli falls in this category and Mn2+ import is specifically induced as a response to oxidative stress.89,90”
From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [89]
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Cites
Cellular Defenses against Superoxide and Hydrogen Peroxide
Imlay, J. A. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061606.161055 · Cited by 1,563 · see citing works
Self-citationToxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
Imlay, J. A., Chin, S. M., & Linn, S. (1988) · Science · doi:10.1126/science.2834821 · Cited by 1,555 · cited 2× · see citing works
“…H2O2 reacts with unincorporated ferrous iron to generate hydroxyl radicals, which then rapidly oxidize nearby biomolecules; when this reaction involves iron that is bound to DNA, mutagenic or lethal lesions can result (Levin et al., 1982; Imlay et al., 1988; Henle et al., 1999; Park et al., 2005).”
BackgroundFemtomolar Sensitivity of Metalloregulatory Proteins Controlling Zinc Homeostasis
Outten, C. E., & O'Halloran, A. T. V. (2001) · Science · doi:10.1126/science.1060331 · Cited by 1,489 · see citing works
The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation
Lee, J.-W., & Helmann, J. D. (2006) · Nature · doi:10.1038/nature04537 · Cited by 547 · see citing works
Lack of a role for iron in the Lyme disease pathogen
Posey, J. E., & Gherardini, F. C. (2000) · Science · doi:10.1126/science.288.5471.1651 · Cited by 538 · see citing works
Horsburgh, M. J., Wharton, S. J., Cox, A. G., Ingham, E., Peacock, S., & Foster, S. J. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02944.x · Cited by 228 · see citing works
Varghese, S., Wu, A., Park, S., Imlay, K. R. C., & Imlay, J. A. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05701.x · Cited by 133 · see citing works
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Research works printed but not linked: 64
- Adams S Green P Claxton R Simcox S Williams MV Walsh K Leeuwenburgh C Reactive carbonyl formation by oxidative and non-oxidative pathways Front Biosci 2001 6 A17 24 11487471
- Al-Maghrebi M Fridovich I Benov L Manganese supplementation relieves the phenotypic deficits seen in superoxide-dismutase-null Escherichia coli Arch. Biochem. Biophys 2002 402 104 109 12051688
- Archibald F Manganese: its acquisition by and function in the lactic acid bacteria Crit. Rev. Microbiol 1986a 13 63 109 3522109
- Archibald F Manganese: its acquisition by and function in the lactic acid bacteria Crit Rev Microbiol (1986b 13 63 109 3522109
- Archibald FS Fridovich I Manganese and defenses against oxygen toxicity in Lactobacillus plantarum J. Bacteriol 1981 145 442 451 6257639 PMC217292
- Archibald FS Fridovich I The scavenging of superoxide radical by manganous complexes 1982 Abstract 6284026
- Aslund F Zheng M Beckwith J Storz G Regulation of the OxyR transcriptional factor by hydrogen peroxide and the cellular thiol-disulfide status Proc. Natl. Acad. Sci. USA 1999 96 6161 6165 10339558 PMC26852
- Barynin VV Whittaker MM Antonyuk SV Lamzin VS Harrison PM Artymiuk PJ Whittaker JW Crystal structure of manganese catalase from Lactobacillus plantarum Structure 2001 9 725 738 11587647
- Berlett BS Chock PB Yim MB Stadtman ER Manganese(II) catalyzes the bicarbonate-dependent oxidation of amino acids by hydrogen peroxide and the amino acid-facilitated dismutation of hydrogen peroxide Proc. Natl. Acad. Sci. USA 1990 87 389 393 2296594 PMC53269
- Beyer WF Jr. Fridovich I In vivo competition between iron and manganese for occupancy of the active site region of the manganese-superoxide dismutase of Escherichia coli J Biol Chem 1991 266 303 308 1985901
- Beyer WF Jr. Reynolds JA Fridovich I Differences between the manganese- and the iron-containing superoxide dismutases of Escherichia coli detected through sedimentation equilibrium, hydrodynamic, and spectroscopic studies Biochemistry 1989 28 4403 4409 2669953
- Bjerrum CJ Canfield DE Ocean productivity before about 1.9 Gyr ago limited by phosphorus adsorption onto iron oxides Nature 2002 417 159 162 12000956
- Carmel-Harel O Storz G Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress Annu. Rev. Microbiol 2000 54 439 461 11018134
- Chang EC Kosman DJ Intracellular Mn(II)-associated superoxide scavenging activity protects Cu,Zn superoxide dismutase-deficient Saccharomyces cerevisiae against dioxygen stress JBC 1989 264 12172 12178 2545701
- Daly MJ Gaidamakova EK Matrosova VY Valilenko A Zhai M Venkateswaran A Hess M Omelchenko MV Kostandarithes HM Makarova KS Wackett LP Fredrickson JK Ghosal D Accumulation of Mn(II) in Deinococcus radiodurans facilitates gama-radiation resistance Science 2004 306 1025 1028 15459345
- Datsenko KA Wanner BL One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products Proc. Natl. Acad. Sci. USA 2000 97 6640 6645 10829079 PMC18686
- Flint DH Tuminello JF Emptage MH The inactivation of Fe-S cluster containing hydro-lyases by superoxide J. Biol. Chem 1993 268 22369 22376 8226748
- Grant RA Filman DJ Finkel SE Kolter R Hogle JM The crystal structure of Dps, a ferritin homolog that binds and protects DNA Nat. Struct. Biol 1998 5 294 303 9546221
- Grass G Franke S Taudte N Nies DH Kucharski LM Maguire ME Rensing C The metal permease ZupT from Escherichia coli is a transporter with a broad substrate spectrum J. Bacteriol 2005 187 1604 1611 15716430 PMC1064025
- Gray B Carmichael AJ Kinetics of superoxide scavenging by dismutase enzymes and manganese mimics determined by electronspin resonance Biochem. J 1992 281 795 802 1311175 PMC1130760
- Haldimann A Wanner BL Conditional-replication, integration, excision, and retrieval plasmid-host systems for gene structure-function studies of bacteria J Bacteriol 2001 183 6384 6393 11591683 PMC100134
- Henle ES Han Z Tang N Rai P Luo Y Linn S Sequence-specific DNA cleavage by Fe2+-mediated Fenton reactions has possible biological implications J. Biol. Chem 1999 274 962 971 9873038
- Horsburgh MJ Wharton SJ Karavolos M Foster SJ Manganese: elemental defence for a life with oxygen? Trends Microbiol 2002b 10 496 501 12419613
- Ilari A Ceci P Ferrari D Rossi G Chiancone E Iron incorporation into E. coli Dps gives rise to a ferritin-like microcrystalline core J. Biol. Chem 2002 277 37619 37623 12163499
- Imlay JA Fridovich I Assay of metabolic superoxide production in Escherichia coli JBC 1991 266 6957 6965 1849898
- Inaoka T Matsumura Y Tsuchido T SodA and manganese are essential for resistance to oxidative stress in growing and sporulating cells of Bacillus subtilis J. Bacteriol 1999 181 1939 1943 10074093 PMC93599
- Jang S Imlay JA Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes J. Biol. Chem 2007 282 929 937 17102132 PMC5136138
- Keele BB Jr. McCord JM Fridovich I Superoxide dismutase from Escherichia coli B. A new manganese-containing enzyme J Biol Chem 1970 245 6176 6181 4921969
- Kehres DG Janakiraman A Slauch JM Maguire ME Regulation of Salmonella enterica serovar Typhimurium mntH transcription by H2O2, Fe2+, and Mn2+ J. Bacteriol 2002a 184 3151 3158 12029030 PMC135095
- Kehres DG Janakiraman A Slauch JM Maguire ME Regulation of Salmonella enterica serovar Typhimurium mntH transcription by H(2)O(2), Fe(2+), and Mn(2+) J Bacteriol 2002b 184 3151 3158 12029030 PMC135095
- Kehres DG Maguire ME Emerging themes in manganese transport, biochemistry and pathogenesis in bacteria FEMS Micro. Rev 2003 27 263 290 12829271
- Kehres DG Zaharik ML Finlay BB Maguire ME The NRAMP proteins of Salmonella typhimurium and Escherichia coli are selective manganese transporters involved in the response to reactive oxygen Mol Microbiol 2000a 36 1085 1100 10844693
- Kehres DG Zaharik ML Finlay BB Maguire ME The NRAMP proteins of Salmonella typhimurium and Escherichia coli are selective manganese transporters involved in the response to reactive oxygen Mol. Microbiol 2000b 36 1085 1100 10844693
- Keyer K Imlay JA Superoxide accelerates DNA damage by elevating free-iron levels PNAS 1996 93 13635 13640 8942986 PMC19375
- Kirby T Blum J Kahane I Fridovich I Distinguishing between Mn-containing and Fe-containing superoxide dismutases in crude extracts of cells Arch Biochem Biophys 1980 201 551 555 6994652
- Kono Y Fridovich I Isolation and characterization of the pseudocatalase of Lactobacillus plantarum J Biol Chem 1983 258 6015 6019 6853475
- Kuo CF Mashino T Fridovich I α,β-dihydroxyisovalerate dehydratase: a superoxide-sensitive enzyme J. Biol. Chem 1987 262 4724 4727 3031031
- Lee JH Yeo WS Roe JH Induction of the sufA operon encoding Fe-S assembly proteins by superoxide generators and hdyrogen peroxide: involvement of OxyR, IHF and an unidentified oxidant-responsive factor Mol. Microbiol 2004 51 1745 1755 15009899
- Levin DE Hollstein M Christman MF Schwiers EA Ames BN A new Salmonella tester strain (TA102) with A.T base pairs at the site of mutation detects oxidative mutagens PNAS 1982 79 7445 7449 6760198 PMC347356
- Liochev SI Fridovich I The role of superoxide in the production of hydroxyl radical: in vitro and in vivo Free Rad Biol Med 1994 16 29 33 8299992
- McCord J Fridovich I Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein) J Biol Chem 1969 244 6049 6055 5389100
- Munroe W Kingsley C Durazo A Gralla EB Imlay JA Srinivasan C Valentine JS Only one of a wide assortment of manganese-containing SOD mimicking compounds rescues the slow aerobic growth phenotypes of both Escherichia coli and Saccharomyces cerevisiae strains lacking superoxide dismutase enzymes J Inorg Biochem 2007 101 1875 1882 17723242 PMC3237304
- Murakami K Tsubouchi R Ogawa MF Yoshino M Oxidative inactivation of reduced NADP-generating enzymes in E. coli: iron-dependent inactivation with affinity cleavage of NADP-isocitrate dehydrogenase Arch. Microbiol 2006 186 385 392 16897033
- Neidhardt FC Umbarger HE Kredich NM Chemical Composition of Escherichia coli Escherichia coli and Salmonella 1996 13 16 ASM Press Washington D C
- Niven DF Ekins A al-Samaurai AA Effects of iron and manganese availability on growth and production of superoxide dismutase by Streptococcus suis Can J Microbiol 1999 45 1027 1032 10696482
- Paget MS Buttner MJ Thiol-based regulatory switches Annu Rev Genet 2003 37 91 121 14616057
- Park S You X Imlay JA Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx- mutants of Escherichia coli Proc. Natl. Acad. Sci. USA 2005 102 9317 9322 15967999 PMC1166606
- Patzer SI Hantke K Dual repression by Fe(2+)-Fur and Mn(2+)-MntR of the mntH gene, encoding an NRAMP-like Mn(2+) transporter in Escherichia coli J Bacteriol 2001 183 4806 4813 11466284 PMC99535
- Pugh SYR DiGuiseppi JL Fridovich I Induction of superoxide dismutases in Escherichia coli by manganese and iron JBact 1984 160 137 142 6384190 PMC214692
- Rai P Cole TD Wemmer DE Linn S Localization of Fe(2+) at an RTGR sequence within a DNA duplex explains preferential cleavage by Fe(2+) and H2O2 J. Mol. Biol 2001 312 1089 1101 11580252
- Runyen-Janecky L Dazenski E Hawkins S Warner L Role and regulation of the Shigella flexneri Sit and MntH systems Infect. Immun 2006 74 4666 4672 16861654 PMC1539580
- Sanchez RJ Srinivasan C Munroe WH Wallace MA Martins J Kao TY Le K Gralla EB Valentine JS Exogenous manganous ion at millimolar levels rescues all known dioxygen-sensitive phenotypes of yeast lacking CuZnSOD J. Biol. Inorg. Chem 2005 10 912 923 16283393
- Seaver LC Imlay JA Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli J. Bacteriol 2001a 183 7173 7181 11717276 PMC95566
- Seaver LC Imlay JA Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli J. Bacteriol 2001b 183 7182 7189 11717277 PMC95567
- Seib KL Tseng HJ McEwan AG Apicella MA Jennings MP Defenses against oxidative stress in Neisseria gonorrhoeae and Neisseria meningitidis: distinctive systems for different lifestyles J Infect Dis 2004 190 136 147 15195253
- Takahashi Y Tokumoto U A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids J. Biol. Chem 2002 277 28380 28383 12089140
- Tardat B Touati D Iron and oxygen regulation of Escherichia coli MnSOD expression. Competition between the global regulators Fur and ArcA for binding to DNA Molecular Microbiology 1993 k9 53 63 8412671
- Tseng HJ McEwan AG Paton JC Jennings MP Virulence of Streptococcus pneumoniae: PsaA mutants are hypersensitive to oxidative stress Infect Immun 2002 70 1635 1639 11854257 PMC127802
- Tseng HJ Srikhanta Y McEwan AG Jennings MP Accumulation of manganese in Neisseria gonorrhoeae correlates with resistance to oxidative killing by superoxide anion and is independent of superoxide dismutase activity Mol. Microbiol 2001 40 1175 1186 11401721
- Whittaker MM Whittaker JW Mutagenesis of a proton linkage pathway in Escherichia coli manganese superoxide dismutase Biochemistry 1997 36 8923 8931 9220980
- Yamakura F Suzuki K Reconstitution of iron-superoxide dismutase Biochem Biophys Res Commun 1976 72 1108 1115 10913
- Yost FJ Jr. Fridovich I An iron-containing superoxide dismutase from Escherichia coli J Biol Chem 1973 248 4905 4908 4352182
- Zheng M Doan B Schneider TD Storz G OxyR and SoxRS regulation of fur J. Bacteriol 1999 181 4639 4643 10419964 PMC103597
- Zheng M Wang X Templeton LJ Smulski DR LaRossa RA Storz G DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide J. Bacteriol 2001 183 4562 4570 11443091 PMC95351
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- Authors
- Anjem, A., Varghese, S., & Imlay, J. A.
- Affiliations
- University of Illinois Urbana-Champaign (US)
- Corresponding author
- Imlay, James A.
- ORCID
- Imlay, James A.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2009-05
- Volume
- 72
- Issue
- 4
- Pages
- 844-858
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- PMC
- PMC2776087
- OpenAlex
- W2159714389
- Cited by
- 324
- References
- 7
- Citations by year
- 2026: 13 · 2025: 12 · 2024: 11 · 2023: 11 · 2022: 18 · 2021: 18 · 2020: 11 · 2019: 14 · 2018: 21 · 2017: 19 · 2016: 16 · 2015: 25 · 2014: 25 · 2013: 27 · 2012: 25
- FWCI
- 10.12
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R37GM049640, GM049640, R01GM049640)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- MntH, hydrogen peroxide stress, oxidative stress resistance, OxyR, Escherichia coli, iron deficiency, Fenton reaction, protein oxidation, iron sequestration
- MeSH terms
- Bacterial Proteins, DNA-Binding Proteins, Escherichia coli, Hydrogen Peroxide, Iron, Manganese, Mutation, Oxidation-Reduction, Repressor Proteins, Superoxide Dismutase, Gene Expression Regulation, Bacterial, Sequence Deletion, Regulon, Oxidative Stress, Cation Transport Proteins, Escherichia coli Proteins, Microbial Viability
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