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Recent Studies on Copper Containing Oxidases

  • B. Mondoví
  • L. Morpurgo
  • G. Rotilio
  • A. Finazzi-Agró
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 74)

Abstract

The role of copper in the oxidizing machinery of life has been recognized long ago. However a detailed knowledge of its function inside proteins is still far from complete and depends on parallel understanding of structure. Malmström et al. (1) first proposed three different types of protein-bound copper, usually referred to as Type 1, Type 2 and Type 3 copper, with special reference to multicopper enzymes such as laccases or ceruloplasmin (2) which contain all the three types. For sake of simplicity we will use this terminology throughout the present paper though, as we will see below, it appears to be rather naive.

Keywords

Carbonic Anhydrase Diamine Oxidase Copper Protein Copper Site Blue Copper 
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).
    Broman, L., Malmström, B.G., Aasa, R. and Vanngard, T. (1962) J. Mol. Biol. 5, 301.PubMedCrossRefGoogle Scholar
  2. 2).
    Malkin, R. and Malmstrom, B.G. (1970) Advances in Enzymology 33, 177–244.Google Scholar
  3. 3).
    Blumberg, W.E. (1966) “Biochemistry of Copper” Blumberg, W.E., Peisach, J. and Aisen, P., Eds., Academic Press Inc., N.Y., pp. 49–66.Google Scholar
  4. 4).
    Brill, A.S. and Brice, G.F. (1968) J. Chem. Phys. 48, 4398–4404.PubMedCrossRefGoogle Scholar
  5. 5).
    Morpurgo, G. and Williams, R.J.P. (1968) “Physiology and Biochemistry of Haemocyanins” Ghiretti, F., Ed., Academic Press, N.Y., pp. 113–130.Google Scholar
  6. 6).
    Gray, H.B. (1971) Adv. Chem. Ser. N. 100, 365.CrossRefGoogle Scholar
  7. 7).
    Miskowsky, V., Tang, S.P.W., Spiro, T.G., Shapiro, E. and Moss, T.H. (1975) Biochemistry 14, 1244–1250.CrossRefGoogle Scholar
  8. 8).
    Falk, K.E. and Reinhammar, B. (1972) Biochim. Biophys. Acta 285, 84–90.PubMedCrossRefGoogle Scholar
  9. 9).
    Rotilio, G., Morpurgo, L., Graziani, M.T. and Brunori, M. (1975) FEBS Letters 54, 163–166.PubMedCrossRefGoogle Scholar
  10. 10).
    Van Leeuwen, F.R., Wever, R., Van Gelder, B.F., Avigliano, L. and Mondoví, B. (1975) Biochim. Biophys. Acta 403, 285–291.PubMedCrossRefGoogle Scholar
  11. 11).
    Avigliano, L., Gerosa, P., Rotilio, G., Finazzi-Agró, A., Calabrese, L. and Mondoví, B. (1972) It. J. Biochem. 21, 248–255.Google Scholar
  12. 12).
    Mondoví, B., Avigliano, L., Rotilio, G., Finazzi-Agro, A., Gerosa, P. and Giovagnoli, C. (1975) Mol. Cell. Biochem. 7, 131–135.PubMedCrossRefGoogle Scholar
  13. 13).
    Lindskog, S., Henderson, L.E., Kannan, K.K., Liljas, A., Nyman, P.O. and Strandberg, B. (1971) “The Enzymes” Vol. 5, pp. 587–665.CrossRefGoogle Scholar
  14. 14).
    Richardson, T.S., Thomas, K.A., Rubin, B.H. and Richardson, D.C. (1975) Proc. Nat. Acad. Sci. U.S.A., 72, 1349–1353.CrossRefGoogle Scholar
  15. 15).
    Jolley, R.L., Evans, L.H., Makino, N. and Mason, H.S. (1974) J. Biol. Chem. 249, 335–345.PubMedGoogle Scholar
  16. 16).
    Van Holde, K.E. (1967) Biochemistry 6, 93–99.PubMedCrossRefGoogle Scholar
  17. 17).
    Coleman, J.E. and Coleman, R.V. (1972) J. Biol. Chem. 247, 4718–4728.PubMedGoogle Scholar
  18. 18).
    Taylor, J.S. and Coleman, J.E. (1971) J. Biol. Chem. 246, 7058–7067.PubMedGoogle Scholar
  19. 19).
    Morpurgo, L., Rotilio, G., Finazzi-Agro, A. and Mondoví, B. (1975) Arch. Biochem. Biophys. 170, 360–366.PubMedCrossRefGoogle Scholar
  20. 20).
    Morpurgo, L., Giovagnoli, C. and Rotilio, G. (1973) Biochim. Biophys. Acta 322, 204–210.PubMedCrossRefGoogle Scholar
  21. 21).
    Shinitzky, M., Katchalski, E., Grisaro, V. and Sharon, N. (1966) Arch. Biochem. Biophys. 116, 332–343.PubMedCrossRefGoogle Scholar
  22. 22).
    Malmström, B.G., Reinhammar, B. and Vänngard, T. (1970) Biochim. Biophys. Acta 205, 48–57.PubMedCrossRefGoogle Scholar
  23. 23).
    Mc Miliin, D.R., Holwerda, R.A. and Gray, H.B. (1974) Proc. Nat. Acad. Sci. U.S.A. 71, 1339–1341.CrossRefGoogle Scholar
  24. 24).
    Elliott, H., Hataway, B.J. and Slade, R.C. (1966) J. Chem. Soc. (A) 1443–1445.Google Scholar
  25. 25).
    Reinhainmar, B. (1972) Biochim. Biophys. Acta 275, 245–259.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • B. Mondoví
    • 1
  • L. Morpurgo
    • 1
  • G. Rotilio
    • 1
  • A. Finazzi-Agró
    • 1
  1. 1.Institutes of Applied Biochemistry and of Biological Chemistry, National Research CouncilUniversity of Rome and Center of Molecular BiologyRomeItaly

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