Iron- and Manganese-Containing Superoxide Dismutases: Structure, Distribution, and Evolutionary Relationships

  • Joe M. McCord
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 74)


In 1969, a well-studied family of mammalian copper-containing proteins was discovered to possess superoxide dismutase activity (1). This rather bizarre activity was postulated to play a protective role for the oxygen-metabolizing organism. Its ubiquity among the various mammalian tissues led us to attempt isolating the activity from an evolutionarily distant species, Escherichia coli (2). Although cell-free extracts of E. coli contained roughly the same amount of superoxide dismutase activity as mammalian tissue extracts, the enzyme’s behaviour during purification bore no resemblance to that of the bovine enzyme. When the enzyme was purified to homogeniety and concentrated, we did not see the familiar blue-green color of the mammalian copper-containing superoxide dismutases. The enzyme was pink. Undaunted, and perhaps comforted by the fact that some copper proteins are pink (3), we set out to determine the copper content of the new superoxide dismutase. No copper could be detected, either by a colorimetric method or by electron paramagnetic resonance (EPR). In fact, no EPR signal at all could be detected in the native protein. Upon denaturation by boiling in 0.1 N HCl, however, the characteristic six-pronged spectrum of manganese(II) appeared.


Electron Paramagnetic Resonance Superoxide Dismutase Electron Paramagnetic Resonance Signal Manganese Superoxide Dismutase Iron Superoxide Dismutases 
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  1. 1.
    McCord, J.M. and Fridovich, I. (1969) J. Biol. Chem. 244:6049–6055.PubMedGoogle Scholar
  2. 2.
    Keele, B.B., Jr., McCord, J.M. and Fridovich, I. (1970) J. Biol. Chem. 245:6176–6181.PubMedGoogle Scholar
  3. 3.
    Reed, D.W., Passon, P.G. and Hultquist, D.E. (1970) J. Biol. Chem. 245:2954–2961.PubMedGoogle Scholar
  4. 4.
    Yost, F.J. and Fridovich, I. (1973) J. Biol. Chem. 248:4905–4908.PubMedGoogle Scholar
  5. 5.
    Vance, P.G., Keele, B.B., Jr. and Rajagopalan, K.V. (1972) J. Biol. Chem. 247:4782–4786.PubMedGoogle Scholar
  6. 6.
    Bridgen, J., Harris, J.I. and Northrop, F. (1975) FEBS Lett. 49:392–395.PubMedCrossRefGoogle Scholar
  7. 7.
    Asada, K., Yoshikawa, K., Takahashi, M., Maeda, Y. and Enmanji, K. (1975) J. Biol. Chem. 250:2801–2807.PubMedGoogle Scholar
  8. 8.
    Puget, K. and Michelson, A.M. (1974) Biochimie 56:1255–1267.PubMedCrossRefGoogle Scholar
  9. 9.
    Lavelle, F., Durosay, P. and Michelson, A.M. (1974) Biochimie 56:451–458.PubMedCrossRefGoogle Scholar
  10. 10.
    Ravindranath, S.D. and Fridovich, I. (1975) J. Biol. Chem. 250: 6107–6112.PubMedGoogle Scholar
  11. 11.
    Weisiger, R.A. and Fridovich, I. (1973) J. Biol. Chem. 248: 3582–3592.PubMedGoogle Scholar
  12. 12.
    McCord, J.M., Rizzolo, L., Boyle, J.A., Day, E.D., Jr. and Salin, M.L., to be published.Google Scholar
  13. 13.
    Misra, H.P. and Keele, B.B., Jr. (1975) Biochim. Biophys. Acta 379:418–425.PubMedCrossRefGoogle Scholar
  14. 14.
    Murphy, J.B. and Kies, M.W. (1960) Biochim. Biophys. Acta 45: 382–384.CrossRefGoogle Scholar
  15. 15.
    Reed, G.H. and Cohn, M. (1970) J. Biol. Chem. 245:662–664.PubMedGoogle Scholar
  16. 16.
    Sastry, G.S., Hamm, R.E. and Pool, K.H. (1969) Anal. Chem. 41: 857–858.CrossRefGoogle Scholar
  17. 17.
    Steinman, H.M. and Hill, R.L. (1973) Proc. Nat. Acad. Sci. USA 70:3725–3729.PubMedCrossRefGoogle Scholar
  18. 18.
    Steinman, H.M., Naik, V.R., Abernethy, J.L. and Hill, R.L. (1974) J. Biol. Chem. 249:7326–7338.PubMedGoogle Scholar
  19. 19.
    Steinman, H.M., preliminary unpublished results.Google Scholar
  20. 20.
    Puget, K. and Michelson, A.M. (1974) Biochem. Biophys. Res. Comm. 58:830–838.PubMedCrossRefGoogle Scholar
  21. 21.
    Gregory, E.M., Yost, F.J., Jr., and Fridovich, I, (1973) J. Bacteriol. 115:987–991.Google Scholar
  22. 22.
    Weisiger, R.A. and Fridovich, I. (1973) J. Biol. Chem. 248: 4793–4796.PubMedGoogle Scholar
  23. 23.
    Tyler, D.D. (1975) Biochem, J. 147:493–504.Google Scholar
  24. 24.
    Peeters-Joris, C., Vandevoorde, A. and Baudhuin, P. (1975) Biochem. J. 150:31–39.PubMedGoogle Scholar
  25. 25.
    Panchenko, L.F., Brusov, O.S., Gerasimov, A.M. and Loktaeva, T.D. (1975) FEBS Lett. 55:84–87.PubMedCrossRefGoogle Scholar
  26. 26.
    Salin, M.L. and McCord, J.M. (1974) J. Clin. Invest. 54:1005–1009.PubMedCrossRefGoogle Scholar
  27. 27.
    Beauchamp, C.O. and Fridovich, I. (1971) Anal. Biochem. 44: 276–287.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • Joe M. McCord
    • 1
  1. 1.Duke University Medical CenterDurhamUSA

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