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Mechanism of Activation and Reduction of Dioxygen by Rhus Laccase — A Blue Copper Oxidase

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Gas Enzymology

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Abstract

The enzymatic reactions of the blue copper oxidase, Rhus laccase are discussed and the importance of dioxygen intermediates coordinated to the type 3 copper site in laccase is demonstrated. Based on the experimental evidence discussed in the paper a reaction scheme for laccase is given which requires O2 reduction through the successive stages \(O_2^ - \to O_2^{2 - } \to \left( {{O^{2 - }} + {O^ - }} \right)\) with laccase molecules reduced to different extents. Intermediates with these dioxygen species coordinated to copper have either been identified or are required by the kinetic data. Isolation of a peroxide coordinated laccase intermediate in the reoxidation of the half reduced enzyme with O2 is especially noteworthy. The 0-0 bondbreaking step is shown to involve cooperation between the type 2 and type 3 sites. Conformational changes controlling the relative rates of different steps have been detected and are discussed.

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References

  1. Fee, J., ‘Copper proteins’, Struct. Bonding, 23, 1, 1975.

    Article  CAS  Google Scholar 

  2. Reinhammar, B., and Malmström, B.G., ‘The ‘blue’ copper-containing oxidases’, in Copper Proteins, Vol. 3 of Metals in Biology, Spiro, T.G. ed., John Wiley & Sons, Inc., New York, 1981.

    Google Scholar 

  3. Farver, O. and Pecht, I., ‘Electron transfer processes of blue copper proteins’, in Copper Proteins, Metal Ions in Biology, Vol. 3, Spiro, Th.G., Ed. John Wiley & Sons, New York, 1981.

    Google Scholar 

  4. Reinhammar, B., ‘Purification and properties of laccase and stellacyanin from Rhus vernicifera’, Biochim. Biophys. Acta, 205, 35, 1970.

    Article  CAS  Google Scholar 

  5. Adman, E.T. and Jensen, L.H., ‘Structural features of azurin at 2.7 Å resolution’, Isr. J. Chem. 21, 8, 1981.

    CAS  Google Scholar 

  6. Freeman, H.C., ‘Electron transfer in blue copper proteins’, in Coordination Chemistry, Vol. 21, Laurent, J.P., Ed., Pergamon Press, Oxford, 1981.

    Google Scholar 

  7. Reinhammar, B., ‘Oxidation-reduction potentials of the electron acceptors in laccases and stellacyanin’, Biochim. Biophys. Acta, 275, 245, 1972.

    Article  CAS  Google Scholar 

  8. Brändén, R., Malmström, B.G., and Vänngård, T., ‘The effect of fluoride on the spectral and catalytic properties of three copper-containing oxidases’, Eur. J. Biochem., 36, 195, 1973.

    Article  Google Scholar 

  9. Holwerda, R.A. and Gray, H.B., ‘Mechanistic studies of the reduction of Rhus vernicifera laccase by hydro-quinone’, J. Am. Chem. Soc., 96, 6008, 1974.

    Article  CAS  Google Scholar 

  10. Peisach, J. and Blumberg, W.E., ‘Structural implications derived from the analysis of EPR spectra of natural and artificial copper proteins’, Arch. Biochem. Biophys., 165, 691, 1974.

    Article  CAS  Google Scholar 

  11. Reinhammar, B., and Vänngård, T., ‘The electron-accepting sites in Rhus vernicifera laccase as studied by anaerobic oxidation-reduction titrations’, Eur. J. Biochem., 18, 463, 1971.

    Article  CAS  Google Scholar 

  12. Andréasson, L.-E., Brändén, R., and Reinhammar, B., ‘Kinetic studies of Rhus vernicifera laccase’, Biochim. Biophys. Acta, 438, 370, 1976.

    Google Scholar 

  13. Meisel, D. and Czapski, G. ‘One-electron transfer equilibria and redox-potentials of radicals studied by pulse radiolysis’, J. Rhys. Chem., 79, 1503, 1975.

    Article  CAS  Google Scholar 

  14. Heckner, K.-H. and Landsberg, R., ‘Standard potentials of the OH radicals’, Z. physikal. Chem., 230, 63, 1965.

    CAS  Google Scholar 

  15. Latimer, W.M., Oxidation Potentials, 2nd. Ed., Prentice-Hall, New York, 1952.

    Google Scholar 

  16. Taube, H., ‘Mechanisms of oxidation with oxygen’, J. Gen Physiol. 49, 29, 1966.

    Article  Google Scholar 

  17. Pecht, I., Farver, O., and Goldberg, M., ‘Electron transfer pathways in blue copper proteins’, Adv. Chem., Ser. No. 162, American Chemical Society, Washington, D.C. 1977.

    Google Scholar 

  18. Henry, Y. and Peisach, J., ‘Photoreduction of Copper Chromophores in Blue Oxidases’, J. Biol. Chem., 253 7751, 1978.

    CAS  Google Scholar 

  19. Greenwood, C., Wilson, M.T., and Brunori, M., ‘Partially reduced mammalian cytochrome oxidase. Reactions with carbon monoxide and oxygen’, Biochem. J., 137, 205, 1974

    CAS  Google Scholar 

  20. Farver, O., Goldberg, M., Lancet, D., and Pecht, I., ‘Oxidative titrations of Rhus vernicifera laccase and its specific interaction with hydrogen peroxide’, Biochem. Biophys. Res. Commun., 73, 494, 1976.

    Article  CAS  Google Scholar 

  21. Farver, O., Goldberg, M., and Pecht, I., ‘Circular dichroic spectrum of the laccase-peroxide derivative’, FEBS Lett., 94, 383, 1978.

    Article  CAS  Google Scholar 

  22. Graziani, M.T., Morpurgo, L., Rotilio, G., and Mondovi, B., ‘Selective removal of Type 2 copper from Rhus vernicifera laccase’, FEBS Lett., 70, 87, 1976.

    Article  CAS  Google Scholar 

  23. Farver, O., Frank, P., and Pecht, I., ‘Peroxide binding to the Type 3 site in Rhus vernicifera Laccase Depleted of Type 2 Copper’, Biochem. Biophys. Res. Comm., 108, 273, 1982.

    Article  CAS  Google Scholar 

  24. Petersson, L., Ångström, J., and Ehrenberg, A., ‘Magnetic susceptibility of lacasses and ceruloplasmin’, Biochim. Biophys. Acta, 526, 311, 1978.

    CAS  Google Scholar 

  25. Farver, O. and Pecht, I., ‘Magnetic susceptibility study of the laccase-peroxide derivative’, FEBS Lett., 108. 436, 1979.

    Article  CAS  Google Scholar 

  26. Dooley, D.M., Scott, R.A., Ellinghaus, J., Solomon, E.I. and Gray, H.B., ‘Magnetic susceptibility studies of laccase and oxyhemocyanin’, Proc. Natl. Acad. USA, 75, 3019, 1978.

    Article  CAS  Google Scholar 

  27. Farver, O., Goldberg, M., and Pecht, I., ‘A circular dichroism study of the reactions of Rhus laccase with dioxygen’. Eur. J. Biochem., 104, 71, 1980.

    Article  CAS  Google Scholar 

  28. Goldberg, M., Farver, O., and Pecht, I., ‘Interaction of Rhus laccase with dioxygen and its reduction intermediates’, J. Biol. Chem., 255, 7353, 1980.

    CAS  Google Scholar 

  29. Caughey, W.S., Wallace, W.J., Volpe, J.A., and Yoshikawa, S., ‘Cytochrome c Oxidase’, in The Enzymes, Boyer, P.D., Ed., vol 13, Academic Press, New York, 1975.

    Google Scholar 

  30. Brändén, R. and Deinum, J., ‘Type 2 copper(II) as a component of the dioxygen reducing site in laccase: evidence from EPR experiments with 17O’, FEBS Lett., 73, 144, 1977.

    Article  Google Scholar 

  31. Brändén, R., Deinum, J., and Coleman, M., ‘A mass spectrometric investigation of the reaction between 18O2 and reduced tree laccase. A differentiation between the two water molecules formed’, FEBS Lett., 89, 180, 1978.

    Article  Google Scholar 

  32. Farver, O. and Goldberg, M., unpublished results.

    Google Scholar 

  33. Goldberg, M., Vuk-Pavlovic, S., and Pecht I., ‘Proton and oxygen-17 magnetic resonance relaxation in Rhus laccase solutions: proton exchange with type 2 copper (II) ligands’ Biochemistry, 19, 5181, 1980.

    Article  CAS  Google Scholar 

  34. Aasa, R., Brändén, R., Deinum, J., Malmström, B.G., Reinhammar, B., and Vänngård, T., ‘A 17O-effect on the EPR spectrum of the intermediate in the dioxygen-laccase reaction’, Biochem. Biophys. Res. Commun., 70, 1204, 1976.

    Article  CAS  Google Scholar 

  35. Brändén, R. and Deinum, J., ‘The effect of pH on the oxygen intermediate and the dioxygen reducing site in blue oxidases’, Biochim. Biophys. Acta, 524, 297, 1978.

    Google Scholar 

  36. Petersen, L.C., and Degn, H., ‘Steady-state kinetics of laccase from Rhus vernicifera’, Biochim. Biophys. Acta, 526, 85, 1978.

    CAS  Google Scholar 

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Authors and Affiliations

  1. Institute of Chemistry, AD, Royal Danish School of Pharmacy, 2, Universitetsparken, DK-2100, Copenhagen ø, Denmark

    Ole Farver

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  1. Ole Farver
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Editors and Affiliations

  1. Institutes of Biochemistry and Chemistry, Odense University, Odense, Denmark

    H. Degn , R. P. Cox  & H. Toftlund ,  & 

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© 1985 D. Reidel Publishing Company

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Farver, O. (1985). Mechanism of Activation and Reduction of Dioxygen by Rhus Laccase — A Blue Copper Oxidase. In: Degn, H., Cox, R.P., Toftlund, H. (eds) Gas Enzymology. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-5279-9_5

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  • DOI: https://doi.org/10.1007/978-94-009-5279-9_5

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-8831-2

  • Online ISBN: 978-94-009-5279-9

  • eBook Packages: Springer Book Archive

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