Gene Symbol: sodC
Description: superoxide dismutase, Cu, Zn, periplasmic
Alias: ECK1642, JW1638
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Yao X, Min H, Lv Z. Response of superoxide dismutase, catalase, and ATPase activity in bacteria exposed to acetamiprid. Biomed Environ Sci. 2006;19:309-14 pubmed
    ..However, this oxidative stress lasts for a relatively short time and does not cause a long-term damage. ..
  2. Benov L, Fridovich I. Induction of the soxRS regulon of Escherichia coli by glycolaldehyde. Arch Biochem Biophys. 2002;407:45-8 pubmed
    ..All of these suggest that superoxide radicals produced by the oxidation of glycolaldehyde played a key role in the induction. ..
  3. Battistoni A, Rotilio G. Isolation of an active and heat-stable monomeric form of Cu,Zn superoxide dismutase from the periplasmic space of Escherichia coli. FEBS Lett. 1995;374:199-202 pubmed
    ..Furthermore the purified enzyme proved to be highly heat-stable and, uniquely among CuZnSODs, protease-sensitive. The latter property may explain the previously described lability of this protein in cell extracts. ..
  4. Berducci G, Mazzetti A, Rotilio G, Battistoni A. Periplasmic competition for zinc uptake between the metallochaperone ZnuA and Cu,Zn superoxide dismutase. FEBS Lett. 2004;569:289-92 pubmed
    ..The effective ZnuA ability to sequester the available zinc ions from the periplasm suggests that zinc-containing cytoplasmic proteins are more important for bacterial viability than the periplasmic ones...
  5. Ojima Y, Nishioka M, Taya M. Metabolic alternations in SOD-deficient Escherichia coli cells when cultivated under oxidative stress from photoexcited titanium dioxide. Biotechnol Lett. 2008;30:1107-13 pubmed publisher
    ..These results suggest that the stress-suffering cells switch the metabolic pathway into a "suppressed aerobiosis", possibly for lowering the generation of reactive oxygen species. ..
  6. Gort A, Ferber D, Imlay J. The regulation and role of the periplasmic copper, zinc superoxide dismutase of Escherichia coli. Mol Microbiol. 1999;32:179-91 pubmed
    ..We found that sodC, the gene that encodes the periplasmic SOD of Escherichia coli, is repressed anaerobically by Fnr and is among the ..
  7. Scotti R, Nicolini L, Stringaro A, Gabbianelli R. A study on prophagic and chromosomal sodC genes involvement in Escherichia coli O157:H7 biofilm formation and biofilm resistance to H2O2. Ann Ist Super Sanita. 2015;51:62-6 pubmed publisher
    Escherichia coli O157:H7 possesses one chromosomal and two prophagic sodC genes encoding for Cu,Zn superoxide dismutases. We evaluated the contribution of sodC genes in biofilm formation and its resistance to hydrogen peroxide...
  8. Benov L, Chang L, Day B, Fridovich I. Copper, zinc superoxide dismutase in Escherichia coli: periplasmic localization. Arch Biochem Biophys. 1995;319:508-11 pubmed
    ..Ultrathin sections of fixed E. coli were treated with the antibody followed by protein A bearing 10-nm gold particles. Electron microscopy revealed that Cu,ZnSOD was largely localized in the periplasm in polar bays. ..
  9. Benov L, Fridovich I. Functional significance of the Cu,ZnSOD in Escherichia coli. Arch Biochem Biophys. 1996;327:249-53 pubmed
    ..DDC augmented this induction. These results indicate that the Cu,ZnSOD provides a defense against oxidative stress, which is more important to the sodA sodB mutant than to its SOD-replete parental strain. ..

More Information


  1. Benov L, Fridovich I. Escherichia coli expresses a copper- and zinc-containing superoxide dismutase. J Biol Chem. 1994;269:25310-4 pubmed
    ..It will now be interesting to explore the phenotypic consequences imposed by the absence of this SOD. ..
  2. Battistoni A, Folcarelli S, Gabbianelli R, Capo C, Rotilio G. The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins. Biochem J. 1996;320 ( Pt 3):713-6 pubmed
    ..The substitution of hydrophobic residues with charged ones at positions located at the dimer interface of all known Cu,Zn superoxide dismutases could be specifically responsible for the monomeric structure of the E. coli enzyme. ..
  3. Korshunov S, Imlay J. Detection and quantification of superoxide formed within the periplasm of Escherichia coli. J Bacteriol. 2006;188:6326-34 pubmed
    ..coli. This endogenous superoxide may create oxidative stress in that compartment and be a primary substrate of CuZnSOD. ..
  4. Sevcenco A, Krijger G, Pinkse M, Verhaert P, Hagen W, Hagedoorn P. Development of a generic approach to native metalloproteomics: application to the quantitative identification of soluble copper proteins in Escherichia coli. J Biol Inorg Chem. 2009;14:631-40 pubmed publisher
    ..coli strengthens the view that the bacterial periplasm contains only a few periplasmic copper proteins, and that the cytosol is devoid of copper proteins. ..
  5. Pesce A, Capasso C, Battistoni A, Folcarelli S, Rotilio G, Desideri A, et al. Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography. J Mol Biol. 1997;274:408-20 pubmed
    ..The molecular surface region involved in subunit dimerization in eukaryotic superoxide dismutases is structurally altered in E_SOD and displays a net polar nature. ..
  6. Puget K, Michelson A. Isolation of a new copper-containing superoxide dismutase bacteriocuprein. Biochem Biophys Res Commun. 1974;58:830-8 pubmed
  7. Imlay K, Imlay J. Cloning and analysis of sodC, encoding the copper-zinc superoxide dismutase of Escherichia coli. J Bacteriol. 1996;178:2564-71 pubmed
    ..We have used the N-terminal protein sequence to isolate the gene encoding this enzyme. The gene, denoted sodC, is located at 37.1 min on the chromosome, adjacent to lhr and sodB...
  8. Lacour S, Landini P. SigmaS-dependent gene expression at the onset of stationary phase in Escherichia coli: function of sigmaS-dependent genes and identification of their promoter sequences. J Bacteriol. 2004;186:7186-95 pubmed
    ..Only seven genes (dps, osmE, osmY, sodC, rpsV, wrbA, and yahO) had previously been recognized as rpoS dependent...
  9. Benov L, Fridovich I. Superoxide dismutase protects against aerobic heat shock in Escherichia coli. J Bacteriol. 1995;177:3344-6 pubmed
    ..This effect is not seen at 53 degrees C, presumably because, at this higher temperature, direct thermolability of vital cell components overrides the effect of superoxide radicals. ..
  10. Benov L, Sage H, Fridovich I. The copper- and zinc-containing superoxide dismutase from Escherichia coli: molecular weight and stability. Arch Biochem Biophys. 1997;340:305-10 pubmed
    ..A parallel was drawn between the E. coli Cu,ZnSOD and FALS varients of human Cu,ZnSOD, which are also relatively unstable and exhibit low affinity for Cu(II). ..
  11. Benov L, Beyer W, Stevens R, Fridovich I. Purification and characterization of the Cu,Zn SOD from Escherichia coli. Free Radic Biol Med. 1996;21:117-21 pubmed
    ..0 Cu/subunit and the specific activity would have been 4800 U/mg. It now appears likely that gram negative bacteria will commonly be found to contain a periplasmic Cu,Zn SOD. ..