Kinetics and Mechanisms of CuI/O2 Reactions

  • Andreas D. Zuberbühler
Chapter

Abstract

Copper proteins are found in each class of enzymes engaged in the interaction with dioxygen. Typical examples are lacease1 as an electron transfer oxidase, tyrosinase2 as an oxygenase and hemocyanin as an oxygen carrier3. Direct interaction of O2 with the reduced enzyme is essential in every case. Unstable dioxygen adducts have long been postulated in enzymatic and low-molecular reaction schemes. They were, however, not really backed by direct experimental observation with the single exceptions of hemocyanin and later tyrosinase4. The situation has dramatically changed with the identification and characterization, first by spectroscopic methods, of pseudoreversible dioxygen adducts or peroxo complexes to low-molecular CuI compounds by Karlin and coworkers5,6. Many speculations have been put to an end upon the structural X-ray characterization of a trans-p-peroxo bridged dicopper(II) complex7 [Cu(L]2O 2 2+ (L = tris[(2-pyriaVl)methyl]amine) and a μ-η2:η2 peroxo complex [Cu(L’)]2 O2 8 (L’ = hydrodotns(3,5-diiopropyl-1-pyrazolyl)borate). Most recently, the η2:η2bmdingmode also has been reported tor oxyhemocyanin9.

Keywords

Activation Enthalpy Activation Entropy Bioinorganic Chemistry Peroxo Complex Dioxygen Binding 
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.
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References

  1. 1.
    M.D. Allendorf, DJ. Spira, E.I. Solomon, Proc. Natl Acad. Sci USA, 82, 3063 (1985).PubMedCrossRefGoogle Scholar
  2. 2.
    H.S. Mason, WJL Folks, E. Peterson, J. Am. Chem Soc, 77, 2914 (1955).CrossRefGoogle Scholar
  3. 3.
    T.B. Freedman, J.S. Loehr, T.M. Loehr, J. Am. Chem. Soc, 98, 2809 (1976).PubMedCrossRefGoogle Scholar
  4. 4.
    R.L. Jolley Jr., LH. Evans, H.S. Mason,Biochem. Biophys. Res. Commun., 46, 878 (1972).PubMedCrossRefGoogle Scholar
  5. 5.
    K.D. Karlin and Y. Gultneh, Prog. Inorg. Chem., 35, 219 (1987), and refc. therein.CrossRefGoogle Scholar
  6. 6.
    K.D. Karlin, Y. Gultneh, J.C. Hayes, R.W. Cruse, J. McKnown, J.P. Hutchinson, J. Zubieta, J. Am Chem. Soc., 106, 2121 (1984).CrossRefGoogle Scholar
  7. 7.
    R.R. Jacobson, Z. Tyeklar, A. Farooq, K.D. Karlin, S. Liu, J. Zubieta, J. Am. Chem. Soc, 110, 3690 (1988)CrossRefGoogle Scholar
  8. 8.
    N. Kitajima, K. Fujisawa, Y. Morooka, K. Toriumi, J. Am. Chem. Soc, 111, 8975 (1989).CrossRefGoogle Scholar
  9. 9.
    K. Magnus, H. Ton-That, J. Inorg. Biochem., 47, 20 (1992).CrossRefGoogle Scholar
  10. 10.
    L. Mi and A.D. Zuberbühler, Hehr. Chim. Acta, 74, 1679 (1991).CrossRefGoogle Scholar
  11. 11.
    R.W. Cruse, S. Kaderli, K.D. Karlin, A.D. Zuberbuhler, J. Am. Chem. Soc., 110, 6882 (1988).CrossRefGoogle Scholar
  12. 12.
    K.D. Karlin and A.D. Zuberbuhler, to be published.Google Scholar
  13. 13.
    K.D. Karlin, N. Wei, B. Jung, S. Kaderli, A.D. Zuberbuhler, J. Am. Chem. Soc., 113, 5868 (1991).CrossRefGoogle Scholar
  14. 14.
    A.D. Zuberbuhler, in Dioxygen Activation and Homogeneous Catalytic Oxidation, L.I. Simandi, Ed., (Elsevier Science Publishers, Amsterdam, 1991), pp. 249–257.CrossRefGoogle Scholar
  15. 15.
    I. Sanyal, R.W. Strange, N.J. Blackburn, K.D. Karlin, J. Am. Chem Soc, 113, 4692 (1991).CrossRefGoogle Scholar
  16. 16.
    A.D. Zuberbuhler, Helv. Chim. Acta, 53, 478 (1970).Google Scholar
  17. 17.
    A.D. Zuberbuhler, in Metal Ions in Biological Systems Vol 5, H. Sigel, Ed., (Marcel Dekker, New York, 1976), pp. 325–368.Google Scholar
  18. 18.
    M. Gûntensperger and A.D. Zuberbuhler, Helv. Chim. Acta, 60, 2584 (1977).CrossRefGoogle Scholar
  19. 19.
    P.M. Henry, Inore. Chem., 5, 688 (1966).CrossRefGoogle Scholar
  20. 20.
    G. Rainoni and A.D. Zuberbuhler, Chimia, 28, 67 (1974).Google Scholar
  21. 21.
    H. Gampp and A.D. Zuberbuhler, Chimia, 32, 54 (1987).Google Scholar
  22. 22.
    L. Mi, A.D. Zuberbuhler, Helv. Chim. Acta, 75, 1547 (1992).CrossRefGoogle Scholar
  23. 23.
    A.D. Zuberbuhler, in Copper Coordination Chemistry: Biochemical & Inorganic Perspectives, K.D. Karlin and J. Zubieta, Eds., (Adenine Press, Guflderland, 1983), pp. 237–258.Google Scholar
  24. 24.
    R.W. Cruse, S. Kaderli, C.J. Meyer, A.D. Zuberbuhler, K.D. Karlin, J. Am. Chem. Soc, 110, 5020 (1988).CrossRefGoogle Scholar
  25. 25.
    H. Gampp, M. Maeder, C.J. Meyer, A.D. Zuberbuhler, Talanta, 32, 257 (1985).PubMedGoogle Scholar
  26. 26.
    R. Bilewicz, S. Kaderli, K.D. Karlin, M. Maeder, N. Wei, A.D. Zuberbuhler, to be published.Google Scholar
  27. 27.
    E. Antonini, M. Brunori, H.A. Kuiper, L. Zolla, Biophys. Chem., 18, 117 (1983);PubMedCrossRefGoogle Scholar
  28. 27a.
    Z. Erel, N. Shaklai, E. Daniel, J. Mol Biol. 64, 341 (1972).CrossRefGoogle Scholar

Copyright information

© Chapman & Hall, Inc. 1993

Authors and Affiliations

  • Andreas D. Zuberbühler
    • 1
  1. 1.Department of Chemistry, Institute of Inorganic ChemistryUniversity of BaselBaselSwitzerland

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