Advertisement

Reactivity of Active Centre Analogues of Cu2Zn2Superoxide Dismutase

  • Ulrich Weser
  • Ralf Miesel
  • Margot Linss
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 264)

Abstract

Active centre analogues of Cu2Zn2superoxide dismutase were devised and successfully employed. Emphasis was placed on the flexible nature of the Superoxide mimicking compounds. Di-Schiff-bases proved most appropri ate to fulfil these requirements. Both structural and functional aspects of the copper binding centre of the intact enzyme were met by these complexes. Nanomolar concentrations of copper coordinated in these complexes were sufficient to inhibit the K3CrO8 induced chemiluminescence identical to the reaction of Cu2Zn2superoxide dismutase.

Keywords

Superoxide Dismutase Hyaluronic Acid Superoxide Dismutase Activity Copper Chelate Nitro Tetrazolium 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    U. Weser, K.-H. Sellinger, E. Lengfelder, W. Werner, and J. Strähle, Structure of Cu2(indomethacin)4 and the reaction with Superoxide in aprotic systems, Biochim. Biophys. Acta, 631:232 (1980).PubMedCrossRefGoogle Scholar
  2. 2.
    R. Brigelius, H.-J. Hartmann, W. Bors, M. Saran, E. Lengfelder, and U. Weser, Superoxide dismutase activity of Cu(Tyr)2 and Cu,Co-erythrocuprein, Z. Physiol. Chem., 356:739 (1975).CrossRefGoogle Scholar
  3. 3.
    U. Deuschle and U. Weser, Copper and inflammation, Prog. Clin. Biochem. Med., 2:99 (1985).Google Scholar
  4. 4.
    M. Linss and U. Weser, The di-Schiff-base of pryidine-2-aldehyde and 1,4-diaminobutane, a flexible Cu(I)/Cu(II) chelator of significant Superoxide dismutase mimetic activity, Inorg. Chim. Acta, 125:117 (1986).Google Scholar
  5. 5.
    M. Linss and U. Weser, Redox behaviour and stability of active centre analogues of Cu2Zn2Superoxide dismutase, Inorg. Chim. Acta, 138:175 (1987).CrossRefGoogle Scholar
  6. 6.
    G. Rotilio, A. Finazzi Agrò, L. Calabrese, F. Bossa, P. Guerrieri, and B. Mondovi, Studies of the metal sites of copper proteins. Ligands of copper in hemocuprein, Biochemistry, 10:616 (1971).PubMedCrossRefGoogle Scholar
  7. 7.
    K.M. Beem, D.C. Richardson, and K.V. Rajagopalan, Metal sites of copper-zinc Superoxide dismutase, Biochemistry, 16:1930 (1977).PubMedCrossRefGoogle Scholar
  8. 8.
    U. Sakaguchi and A.W. Addison, Spectroscopic and redox studies of some copper(II) complexes with biomimetic donor atoms: implications for protein copper centers, J. Chem. Soc., Dalton Tran., 4:600 (1979).CrossRefGoogle Scholar
  9. 9.
    G.D. Lawrence and D.T. Sawyer, Potentiometric titrations and oxidation-reduction potenials of manganese and copper-zinc Superoxide dismutase, Biochemistry, 18:3045 (1979).PubMedCrossRefGoogle Scholar
  10. 10.
    U. Weser, C. Richter, A. Wendel, and M. Younes, Reactivity of anti-inflammatory and superoxide dismutase active Cu(II)-salicylates, Bioinorg. Chem., 8:201 (1978).CrossRefGoogle Scholar
  11. 11.
    M. Younes and U. Weser, Inhibition of nitroblue tetrazolium reduction by cuprein (superoxide dismutase), Cu(tyr)2 and Cu(lys)2, FEBS Lett., 61:209 (1976).CrossRefGoogle Scholar
  12. 12.
    U. Weser, W. Paschen, and M. Younes, Singlet oxygen and superoxide dismutase (cuprein), Biochem. Biophys. Res. Commun., 66:769 (1975).PubMedCrossRefGoogle Scholar
  13. 13.
    R. Miesel and U. Weser, Reactivity of active centre analogues of Cu2Zn2superoxide dismutase during the aqueous decay of K3CrO8, Inorg. Chim. Acta, in the press (1989).Google Scholar
  14. 14.
    R. Brigelius, R. Spöttl, W. Bors, E. Lengfelder, M. Saran, and U. Weser, Superoxide dismutase activity of low molecular weight Cu2+ chelates studied by pulse radiolysis, FEBS Lett., 47:72 (1974).PubMedCrossRefGoogle Scholar
  15. 15.
    M. Younes, E. Lengfelder, S. Zienau, and U. Weser, Pulse radiolytically generated superoxide and Cu(ll)-salicylates, Biochem. Biophys. Res. Commun., 81:576 (1978).PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Ulrich Weser
    • 1
  • Ralf Miesel
    • 1
  • Margot Linss
    • 1
  1. 1.Anorganische Biochemie, Physiologisch-Chemisches InstitutUniversität TübingenTübingenGermany

Personalised recommendations