Skip to main content
SpringerLink
Log in

Neurospora tyrosinase: structural, spectroscopic and catalytic properties

  • Published:
Molecular and Cellular Biochemistry Aims and scope Submit manuscript

Summary

Tyrosinase is a copper containing monooxygenase catalyzing the formation of melanin pigments and other polyphenolic compounds from various phenols. This review deals with the recent progress on the molecular structure of the enzyme from Neurospora crassa and the unique features of the binuclear active site copper complex involved in the activation of molecular oxygen and the binding of substrates. The results of the spectroscopic properties of Neurospora tyrosinase will also be discussed in the light of the structural similarity of the copper complex in the oxygen binding hemocyanins.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Mason, H. S., 1965. Annu. Rev. Biochem. 34: 595–634.

    Google Scholar 

  2. Vanneste, W. H. and Zuberbühler, A., 1974. In: Molecular Mechanisms of Oxygen Activation (Hayaishi, O., ed.), pp. 371–404, New York: Academic Press.

  3. Lerch, K., 1981. In: Metal Ions in Biological Systems (Sigel, H., ed.), Vol. 13, pp. 143–186, New York: Marcel Dekker.

  4. Mason, H. S., Fowlks, W. B. and Peterson, E. W., 1955. J. Am. Chem. Soc. 77: 2914–2915.

    Google Scholar 

  5. Bertrand, G., 1895. Compt. rend. 122: 1215–1218.

    Google Scholar 

  6. Nelson, J. M. and Dawson, C. R., 1944. Advances in Enzymol. 4: 99–152.

    Google Scholar 

  7. Dawson, C. R. and Mallette, M. F., 1945. Advances in Protein Chem. 2: 179–248.

    Google Scholar 

  8. Mason, H. S., 1955. Advances in Enzymol. 16: 105–184.

    Google Scholar 

  9. Kubowitz, F., 1938. Biochem. Z. 299: 32–57.

    Google Scholar 

  10. Keilin, D. and Mann, T., 1938. Proc. Roy. Soc. B 125: 187–204.

    Google Scholar 

  11. Hirsch, M. M., 1954. Physiol. Plantarum 7: 72–97.

    Google Scholar 

  12. Horowitz, N. H. and Shen, S. C., 1952. J. Biol. Chem. 197: 513–520.

    Google Scholar 

  13. Horowitz, N. H., Feldman-Macleod, H. L. and Pall, M. L., 1970. J. Biol. Chem. 245: 2784–2788.

    Google Scholar 

  14. Horowitz, N. H., Fling, M., Macleod, H. L. and Sueoka, N., 1960. J. Mol. Biol. 2: 96–104.

    Google Scholar 

  15. Horowitz, N. H., Fling, M., Feldman-Macleod, H., Pall, M. L. and Froehner, S. C., 1970. Devel. Biol. 21: 147–156.

    Google Scholar 

  16. Feldman, J. F. and Thayer, J. P., 1974. Biochem. Biophys. Res. Commun. 61: 977–982.

    Google Scholar 

  17. Horowitz, N. H., Fling, M., Macleod, H. L. and Watanabe, Y., 1961. Cold Spring Harbor Symp. Quant. Biol. 26: 233–238.

    Google Scholar 

  18. Horowitz, N. H., Fling, M., Macleod, H. L. and Sueoka, N., 1961. Genetics 46: 1015–1024.

    Google Scholar 

  19. Fling, M., Horowitz, N. H. and Heinemann, S. F., 1963. J. Biol. Chem. 238: 2045–2053.

    Google Scholar 

  20. Gutteridge, S. and Robb, D., 1975. Eur. J. Biochem. 54: 107–116.

    Google Scholar 

  21. Lerch, K., 1976. FEBS Lett. 69: 157–160.

    Google Scholar 

  22. Deinum, J., Lerch, K. and Reinhammar, B., 1976. FEBS Lett. 69: 161–164.

    Google Scholar 

  23. Lerch, K., 1978. Proc. Natl. Acad. Sci. U.S.A. 75: 3635–3639.

    Google Scholar 

  24. Lerch, K., Longoni, C. and Jordi, E., 1982. J. Biol. Chem. 257: 6408–6413.

    Google Scholar 

  25. Lerch, K., 1982. J. Biol. Chem. 257: 6414–6419.

    Google Scholar 

  26. Nau, H., Lerch, K. and Witte, L., 1977. FEBS Lett. 79: 203–206.

    Google Scholar 

  27. Fox, A. S. and Burnett, J. B.,1959. In: Pigment Cell Biology (Gordon, M., ed.), pp. 249–278, New York: Academic Press.

  28. Rüegg, C., Ammer, D. and Lerch, K., 1982. J. Biol. Chem. 257: 6420–6426.

    Google Scholar 

  29. Pfiffner, E. and Lerch, K., 1981. Biochemistry 21: 6029–6035.

    Google Scholar 

  30. Brooks, D. W. and Dawson, C. R., 1966. In: The Biochemistry of Copper (Peisach, J., Aisen, P. and Blumberg, W. E., eds.), pp. 343–357, New York: Academic Press.

  31. Ingraham, L. L., 1959. In: Pigment Cell Biology (Gordon, M., ed.), pp. 609–617, New York: Academic Press.

  32. Wood, B. J. B. and Ingraham, L. L., 1965. Nature 205: 291–292.

    Google Scholar 

  33. Dietler, C. and Lerch, K., 1982. In: Oxidases and Related Redox Systems (King, T. E., Mason, H. S. and Morrison, M., eds.), pp. 305–317, New York: Pergamon Press.

  34. Rüegg, C. and Lerch, K., 1981. Biochemistry 20: 1256–1262.

    Google Scholar 

  35. Eickman, N. C., Solomon, E. I., Larrabee, J. A., Spiro, T. G. and Lerch, K., 1978. J. Am. Chem. Soc. 100: 6529–6531.

    Google Scholar 

  36. Himmelwright, R. S., Eickman, N. C., LuBien, C. D., Lerch, K. and Solomon, E. I., 1980. J. Am. Chem. Soc. 162: 7339–7344.

    Google Scholar 

  37. Schoot Uiterkamp, A. J. M. and Mason, H. S., 1973. Proc. Natl. Acad. Sci. U.S.A. 70: 993–996.

    Google Scholar 

  38. Jolley, R. L., Jr., Evans, L. H., Makino, N. and Mason, H. S., 1974. J. Biol. Chem. 249: 335–345.

    Google Scholar 

  39. Makino, N., McMahill, P., Mason, H. S. and Moss, T. H., 1974. J. Biol. Chem. 249: 6062–6066.

    Google Scholar 

  40. Eickman, N. C., Himmelwright, R. S. and Solomon, E. I., 1979. Proc. Natl. Acad. Sci. U.S.A. 76: 2094–2098.

    Google Scholar 

  41. Powers, L., Spiro, T. G., Winkler, M. E., Lerch, K. and Solomon, E. L, 1982. (Unpublished results).

  42. Larrabee, J. A. and Spiro, T. G., 1980. J. Am. Chem. Soc. 102: 4217–4223.

    Google Scholar 

  43. Brown, J. M., Powers, L., Kincaid, B., Larrabee, J. A. and Spiro, T. G., 1980. J. Am. Chem. Soc. 102: 4210–4216.

    Google Scholar 

  44. Beltramini, M. and Lerch, K., 1982. Biochem. J. 205: 173–180.

    Google Scholar 

  45. Kuiper, H. A., Lerch, K., Brunori, M. and Finazzi-Agrò, A., 1980. FEBS Lett. 111: 232–334.

    Google Scholar 

  46. Kuiper, H. A., Finazzi-Agrò, A., Antonini, E. and Brunori, M., 1980. Proc. Natl. Acad. Sci. U.S.A. 77: 2387–2389.

    Google Scholar 

  47. Healey, D. F. and Strothkamp, K. G., 1981. Arch. Biochem. Biophys. 211: 86–91.

    Google Scholar 

  48. Rich, P. R., Wiegand, N. K., Blum, H., Moore, A. L. and Bonner, W. D., Jr., 1978. Biochim. Biophys. Acta 525: 325–337.

    Google Scholar 

  49. Hashiguchi, H. and Takayashi, H., 1977. Mol. Pharmacol. 13: 363–367.

    Google Scholar 

  50. Winkler, M. E., Lerch, K. and Solomon, E. I., 1981. J. Am. Chem. Soc. 103: 7001–7003.

    Google Scholar 

  51. Aasa, R., Deinum, J., Lerch, K. and Reinhammar, B., 1978. Biochim. Biophys. Acta 535: 287–298.

    Google Scholar 

  52. Peisach, J. and Blumberg, W. E., 1974. Arch. Biochem. Biophys. 165: 691–708.

    Google Scholar 

  53. Lerch, K., Mims, W. B. and Peisach, J., 1981. J. Biol. Chem. 256: 10088–10091.

    Google Scholar 

  54. Makino, N. and Mason, H. S., 1973. J. Biol. Chem. 248: 5731–5735.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Biochemisches Institut der Universität Zürich, Zürichbergstrasse 4, CH-8028, Zürich, Switzerland

    Konrad Lerch

Authors
  1. Konrad Lerch
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Lerch, K. Neurospora tyrosinase: structural, spectroscopic and catalytic properties. Mol Cell Biochem 52, 125–138 (1983). https://doi.org/10.1007/BF00224921

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00224921

Keywords

Search

Navigation