Gene Symbol: SOD1
Description: superoxide dismutase 1
Alias: SOD1L1, superoxide dismutase [Cu-Zn], Cu-Zn superoxide dismutase, superoxide dismutase 1, soluble
Species: cow
Products:     SOD1

Top Publications

  1. Tainer J, Getzoff E, Richardson J, Richardson D. Structure and mechanism of copper, zinc superoxide dismutase. Nature. 1983;306:284-7 pubmed
    ..The geometry and molecular surface of the active site, together with biochemical data, suggest a specific model for the enzyme mechanism. ..
  2. Agbas A, Hui D, Wang X, Tek V, Zaidi A, Michaelis E. Activation of brain calcineurin (Cn) by Cu-Zn superoxide dismutase (SOD1) depends on direct SOD1-Cn protein interactions occurring in vitro and in vivo. Biochem J. 2007;405:51-9 pubmed
    Cn (calcineurin) activity is stabilized by SOD1 (Cu-Zn superoxide dismutase), a phenomenon attributed to protection from superoxide (O2*-). The effects of O2*- on Cn are still controversial...
  3. Lee S, Acosta T, Nakagawa Y, Okuda K. Role of nitric oxide in the regulation of superoxide dismutase and prostaglandin F(2alpha) production in bovine luteal endothelial cells. J Reprod Dev. 2010;56:454-9 pubmed
  4. Moyes K, Drackley J, Morin D, Loor J. Greater expression of TLR2, TLR4, and IL6 due to negative energy balance is associated with lower expression of HLA-DRA and HLA-A in bovine blood neutrophils after intramammary mastitis challenge with Streptococcus uberis. Funct Integr Genomics. 2010;10:53-61 pubmed publisher NEB were ALOX5AP, CPNE3, IL1R2, IL6, TLR2, TLR4, and THY1, and downregulated genes were HLA-DRA, HLA-A, IRAK1, SOD1, and TNF...
  5. Gunther M, Donahue J. Bicarbonate and active site zinc modulate the self-peroxidation of bovine copper-zinc superoxide dismutase. Free Radic Res. 2007;41:1005-16 pubmed
    Peroxidation reactions of copper-zinc superoxide dismutase (CuZn-SOD1) or its zinc-depleted form (CuE-SOD1) that likely also involve a component of bicarbonate buffer have been implicated in the pathophysiology of the neurodegenerative ..
  6. Steinman H, Naik V, Abernethy J, Hill R. Bovine erythrocyte superoxide dismutase. Complete amino acid sequence. J Biol Chem. 1974;249:7326-38 pubmed
  7. Abernethy J, Steinman H, Hill R. Bovine erythrocyte superoxide dismutase. Subunit structure and sequence location of the intrasubunit disulfide bond. J Biol Chem. 1974;249:7339-47 pubmed
  8. Potter S, Zhu H, Shaw B, Rodriguez J, Doucette P, Sohn S, et al. Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein. J Am Chem Soc. 2007;129:4575-83 pubmed
    The thermodynamics of zinc binding to metal-free (apo) human and bovine copper-zinc superoxide dismutases (SOD1) were measured using isothermal titration calorimetry...
  9. Kankofer M, Wawrzykowski J, Hoedemaker M. The presence of SOD 1 and GSH-Px in bovine retained and properly released foetal membranes. Reprod Domest Anim. 2013;48:699-704 pubmed publisher
    ..Local antioxidative enzymatic mechanisms in bovine placental tissues are represented by CuZn-SOD and cGSH-Px, which show the changes in their expression during improper placental release. ..

More Information


  1. Ye M, English A. Binding of polyaminocarboxylate chelators to the active-site copper inhibits the GSNO-reductase activity but not the superoxide dismutase activity of Cu,Zn-superoxide dismutase. Biochemistry. 2006;45:12723-32 pubmed
    ..This induces a conformational change at the second active site that inhibits the GSNO-reductase but not the SOD activity of the enzyme. ..
  2. Taoufiq Z, Pino P, Dugas N, Conti M, Tefit M, Mazier D, et al. Transient supplementation of superoxide dismutase protects endothelial cells against Plasmodium falciparum-induced oxidative stress. Mol Biochem Parasitol. 2006;150:166-73 pubmed
    ..Cytoplasmic Cu/Zn superoxide dismutase (SOD1), which provides the first line of defense against oxidative stress within a cell, is now used as a treatment of ..
  3. Hough M, Hasnain S. Crystallographic structures of bovine copper-zinc superoxide dismutase reveal asymmetry in two subunits: functionally important three and five coordinate copper sites captured in the same crystal. J Mol Biol. 1999;287:579-92 pubmed
    ..We also suggest that the increased separation between Cu and Zn is a precursor to breakage of His61. ..
  4. Karunakaran C, Zhang H, Crow J, Antholine W, Kalyanaraman B. Direct probing of copper active site and free radical formed during bicarbonate-dependent peroxidase activity of bovine and human copper, zinc-superoxide dismutases. Low-temperature electron paramagnetic resonance and electron nuclear double resonanc. J Biol Chem. 2004;279:32534-40 pubmed
    ..The time course EPR of wild type human SOD1 (WT hSOD1), W32F hSOD1 mutant (tryptophan 32 substituted with phenylalanine), and bSOD1 treated with H(2)O(2) and ..
  5. Richardson J, Thomas K, Rubin B, Richardson D. Crystal structure of bovine Cu,Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands. Proc Natl Acad Sci U S A. 1975;72:1349-53 pubmed
    ..The overall folding pattern of the polypeptide chain is very similar to that of an immunoglobulin domain. ..
  6. Jiang W, Han Y, Zhou R, Zhang L, Liu C. DNA is a template for accelerating the aggregation of copper, zinc superoxide dismutase. Biochemistry. 2007;46:5911-23 pubmed
    The proteinaceous aggregates rich in copper, zinc superoxide dismutase (SOD1) have been shown to be involved in pathogenesis of amyotrophic lateral sclerosis (ALS)...
  7. Oneda H, Inouye K. Effect of nitration on the activity of bovine erythrocyte Cu,Zn-superoxide dismutase (BESOD) and a kinetic analysis of its dimerization-dissociation reaction as examined by subunit exchange between the native and nitrated BESODs. J Biochem. 2003;134:683-90 pubmed
    ..0 to 10.0, but increased remarkably with a decrease in the dielectric constant of the reaction mixture. It is suggested that hydrophobic interaction may play a significant role in the subunit interaction. ..
  8. Gibbs L, Shaffer J. Nucleotide sequence of bovine copper/zinc superoxide dismutase cDNA generated by the polymerase chain reaction. Nucleic Acids Res. 1990;18:7171 pubmed
  9. Tainer J, Getzoff E, Beem K, Richardson J, Richardson D. Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase. J Mol Biol. 1982;160:181-217 pubmed
  10. Malinowski D, Fridovich I. Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase. Biochemistry. 1979;18:5909-17 pubmed
  11. Schmutz S, Cornwell D, Moker J, Troyer D. Physical mapping of SOD1 to bovine chromosome 1. Cytogenet Cell Genet. 1996;72:37-9 pubmed
    Superoxide dismutase 1 (SOD1) was mapped to cattle chromosome 1q12 --> q14 by in situ methods...
  12. Ramirez D, Gomez Mejiba S, Mason R. Mechanism of hydrogen peroxide-induced Cu,Zn-superoxide dismutase-centered radical formation as explored by immuno-spin trapping: the role of copper- and carbonate radical anion-mediated oxidations. Free Radic Biol Med. 2005;38:201-14 pubmed
    We have reinvestigated the biochemistry of H2O2-induced Cu,Zn-superoxide dismutase (SOD1)-centered radicals, detecting them by immuno-spin trapping...
  13. Harraz M, Marden J, Zhou W, Zhang Y, Williams A, Sharov V, et al. SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model. J Clin Invest. 2008;118:659-70 pubmed publisher
    ..sclerosis (ALS) is associated with enhanced redox stress caused by dominant mutations in superoxide dismutase-1 (SOD1). SOD1 is a cytosolic enzyme that facilitates the conversion of superoxide (O(2)(*-)) to H(2)O(2)...
  14. Zhu J, Zhang X, Roneker C, McClung J, Zhang S, Thannhauser T, et al. Role of copper,zinc-superoxide dismutase in catalyzing nitrotyrosine formation in murine liver. Free Radic Biol Med. 2008;45:611-8 pubmed publisher
    The only known function of Cu,Zn-superoxide dismutase (SOD1) is to catalyze the dismutation of superoxide anion into hydrogen peroxide...
  15. Hong J, Moosavi Movahedi A, Ghourchian H, Amani M, Amanlou M, Chilaka F. Thermal dissociation and conformational lock of superoxide dismutase. J Biochem Mol Biol. 2005;38:533-8 pubmed
    ..It is suggested that the contact areas interact with active centers by conformational changes involving secondary structural elements. ..
  16. Hough M, Hasnain S. Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 A. Structure. 2003;11:937-46 pubmed
    ..65 A) has allowed a more detailed examination of the metal center environment and its associated water network in the active site channel, facilitating the analysis of potential proton transfer routes. ..
  17. Jiang W, Zhang B, Yin J, Liu L, Wang L, Liu C. Polymorphism of the SOD1-DNA aggregation species can be modulated by DNA. Biopolymers. 2008;89:1154-69 pubmed publisher
    Proteinaceous aggregates rich in copper, zinc superoxide dismutase (SOD1) have been found in both in vivo and in vitro models...
  18. Hallewell R, Imlay K, Lee P, Fong N, Gallegos C, Getzoff E, et al. Thermostabilization of recombinant human and bovine CuZn superoxide dismutases by replacement of free cysteines. Biochem Biophys Res Commun. 1991;181:474-80 pubmed
    ..In all cases, removal of a free cysteine residue increased thermostability. ..
  19. Ascone I, Savino C, Kahn R, Fourme R. Flexibility of the Cu,Zn superoxide dismutase structure investigated at 0.57 GPa. Acta Crystallogr D Biol Crystallogr. 2010;66:654-63 pubmed publisher
    ..This work illustrates the potential of combining X-ray crystallography with high pressure to promote and stabilize higher energy conformational substates. ..
  20. Borges Alvarez M, Benavente F, Barbosa J, Sanz Nebot V. Capillary electrophoresis/mass spectrometry for the separation and characterization of bovine Cu,Zn-superoxide dismutase. Rapid Commun Mass Spectrom. 2010;24:1411-8 pubmed publisher
    ..Our results highlight the importance of selecting appropriate non-denaturing separation and detection conditions to obtain reliable structural information about non-covalent protein complexes by CE/ESI-MS. ..
  21. Ramasarma T, Rao A, Devi M, Omkumar R, Bhagyashree K, Bhat S. New insights of superoxide dismutase inhibition of pyrogallol autoxidation. Mol Cell Biochem. 2015;400:277-85 pubmed publisher
    ..SOD catalyzes reversal of autoxidation manifesting as its inhibition. SOD saves catechols from autoxidation and extends their bioavailability. ..
  22. Uehara H, Luo S, Aryal B, Levine R, Rao V. Distinct oxidative cleavage and modification of bovine [Cu- Zn]-SOD by an ascorbic acid/Cu(II) system: Identification of novel copper binding site on SOD molecule. Free Radic Biol Med. 2016;94:161-73 pubmed publisher
    ..hydrogen peroxide on the cleavage and oxidation indicated that binding of copper to a previously unknown site on SOD1 is responsible for the Asc/Cu(II) specific cleavage and oxidation...
  23. Toyama A, Takahashi Y, Takeuchi H. Catalytic and structural role of a metal-free histidine residue in bovine Cu-Zn superoxide dismutase. Biochemistry. 2004;43:4670-9 pubmed
  24. Vu H, Lee S, Acosta T, Yoshioka S, Abe H, Okuda K. Roles of prostaglandin F2alpha and hydrogen peroxide in the regulation of Copper/Zinc superoxide dismutase in bovine corpus luteum and luteal endothelial cells. Reprod Biol Endocrinol. 2012;10:87 pubmed publisher
    ..and ROS in bovine corpus luteum (CL) during luteolysis, we determined the time-dependent change of Copper/Zinc SOD (SOD1) in CL tissues after PGF treatment in vivo...
  25. Jiao M, Li H, Chen J, Minton A, Liang Y. Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria. Biophys J. 2010;99:914-23 pubmed publisher
  26. Bonini M, Gabel S, Ranguelova K, Stadler K, Derose E, London R, et al. Direct magnetic resonance evidence for peroxymonocarbonate involvement in the cu,zn-superoxide dismutase peroxidase catalytic cycle. J Biol Chem. 2009;284:14618-27 pubmed publisher
    Cu,Zn-superoxide dismutase (SOD1) is a copper- and zinc-dependent enzyme. The main function of SOD1 is believed to be the scavenging and detoxification of superoxide radicals...
  27. Rypniewski W, Mangani S, Bruni B, Orioli P, Casati M, Wilson K. Crystal structure of reduced bovine erythrocyte superoxide dismutase at 1.9 A resolution. J Mol Biol. 1995;251:282-96 pubmed
    ..There are significant differences between the active sites of the two crystallographically independent monomers. They are explained in terms of local differences in the crystal environment. ..
  28. Kim Y, Nakatomi R, Akagi T, Hashikawa T, Takahashi R. Unsaturated fatty acids induce cytotoxic aggregate formation of amyotrophic lateral sclerosis-linked superoxide dismutase 1 mutants. J Biol Chem. 2005;280:21515-21 pubmed
    ..Superoxide dismutase 1 (SOD1) immunoreactive inclusions have been found in the spinal cord of ALS animal models and patients, implicating the ..
  29. Combelles C, Holick E, Paolella L, Walker D, Wu Q. Profiling of superoxide dismutase isoenzymes in compartments of the developing bovine antral follicles. Reproduction. 2010;139:871-81 pubmed publisher
    ..We thus evaluated the expression of the three isoforms (SOD1, SOD2, and SOD3) of the enzymatic antioxidant superoxide dismutase in all the cellular (granulosa cells, cumulus ..
  30. Djinovic K, Coda A, Antolini L, Pelosi G, Desideri A, Falconi M, et al. Crystal structure solution and refinement of the semisynthetic cobalt-substituted bovine erythrocyte superoxide dismutase at 2.0 A resolution. J Mol Biol. 1992;226:227-38 pubmed
  31. Roy M, Gauvreau D, Bilodeau J. Expression of superoxide dismutases in the bovine oviduct during the estrous cycle. Theriogenology. 2008;70:836-42 pubmed publisher
    ..objective was to characterize, by western blot analysis, the expression of two SODs, the cytosolic (Cu,ZnSOD or SOD1) and the mitochondrial (MnSOD or SOD2) forms in three sections of the oviduct, i.e...