Skip to main content

On the Active Site of Molluscan Haemocyanin and of Tyrosinases. Opening Address

  • Conference paper
Structure and Function of Haemocyanin

Part of the book series: Proceedings in Life Sciences ((LIFE SCIENCES))

Abstract

In the next Haemocyanin Workshop we ought to celebrate the centennial of the terms “haemocyanin” and “oxyhaemocyanin”, coined in 1878 by Leon Fredericq (1851–1935), who later became professor of physiology at the State University of Liege. Préparateur at the time at the State University of Ghent, he spent the second half of July and the month of August 1878 at the newly established laboratory in Roscoff, Brittany, working on the physiology of the octopus (Florkin, 1943). He realized that the colourless blood substance, a protein, became blue on binding oxygen reversibly and acted as an oxygen carrier. He could not detect any iron, but found instead the presence of copper (Fredericq, 1878).

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

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Bannister, W.H., Wood, E.J.: Free electron model for the absorption of oxygen-bridged binuclear complexes in the near ultraviolet. Nature (London) 223, 53–54 (1969)

    Article  CAS  Google Scholar 

  • Bannister, W.H., Wood, E.J.: Gaussian analysis of the visible and near-ultraviolet absorption and circular dichroism spectra of haemocyanin from Murex trunculus. Comp. Biochem. Physiol. 43B, 1033–1037 (1972)

    Google Scholar 

  • Bonaventura, C., Sullivan, B., Bonaventura, J., Bourne, S.: CO binding by hemocyanins of Limulus polyphenols, Busyoon cavica, and Callineotes sapidus. Biochemistry 13., 4784–4789 (1974)

    Article  PubMed  CAS  Google Scholar 

  • Cox, J.A., Elliott, F.G.: Isotopic copper exchange in Vila haemocyanin with three radioactive cuprous complexes. Biochim. Biophys. Acta 371, 392–401 (1974)

    PubMed  CAS  Google Scholar 

  • De Ley, M., Candreva, F., Witters, R., Lontie, R.: The fast reduction of Helix pomatia methaemocyanin with hydrogen sulphide. FEBS Lett. 57, 234–236 (1975)

    Article  PubMed  CAS  Google Scholar 

  • Dhéré, Ch.: Sur quelques pigments respiratoires des Invertebres. Revue Suisse Zool. 35, 277–288 (1928)

    Google Scholar 

  • Fager, L.Y., Alben, J.O.: Structure of the carbon monoxide binding site of hemocyanins studied by Fourier transform infrared spectroscopy. Biochemistry 11, 4786–4792 (1972)

    Article  PubMed  CAS  Google Scholar 

  • Felsenfeld, G., Printz, M.P.: Specific reactions of hydrogen peroxide with the active site of hemocyanin. The formation of “methemocyanin”. J. Am. Chem. Soc. 81, 6259– 6264 (1959)

    Article  CAS  Google Scholar 

  • Florkin, M.: Leon Fredericq et les Debuts de la Physiologie en Belgique. Brussels: Office de Publicite, 1943, p. 32

    Google Scholar 

  • Fredericq, L.: Sur 1’hemocyanine, substance nouvelle due sang de Poupe [Octopus Vulgaris). C. R. Acad. Sci. (Paris) 87, 996–998 (1878)

    Google Scholar 

  • Freedman, T.B., Loehr, J.S., Loehr, T.M.: A resonance Raman study of the copper protein, hemocyanin. New evidence for the structure of the oxygen-binding site. J. Am. Chem. Soc. 98, 2809–2815 (1976)

    Article  PubMed  CAS  Google Scholar 

  • Freeman, H.C.: Crystal structures of metal-peptide complexes. Advan. Protein Chem. 22, 257–424 (1967)

    Article  CAS  Google Scholar 

  • Ghiretti, F.: The decomposition of hydrogen peroxide by Octopus hemocyanin. Bull. Soc. Chim. Belg. 65, 103–106 (1956)

    Article  CAS  Google Scholar 

  • Gielens, C., Preaux, G., Lontie, R. : Limited trypsinolysis of β-haemocyanin of Helix pomatia. Characterization of the fragments and heterogeneity of the copper groups by circular dichroism. Europ. J. Biochem. 60, 271–280 (1975)

    Article  PubMed  CAS  Google Scholar 

  • Gray, H.B.: Polynuclear iron (III) complexes. In: Proteins of Iron Storage and Transport in Biochemistry and Medicine. Crichton, R.R. (ed.). Amsterdam-Oxford: North-Holland, 1975, p. 7

    Google Scholar 

  • Guillemet, R., Gosselin, G.: Sur le rapport entre le cuivre et la capacite’ respira- toire dans les sangs hemocyaniques. C. R. Soc. Biol. 111, 733–735 (1932)

    CAS  Google Scholar 

  • Henriksson, H.-Å., Sjoberg, B., Osterberg, R.: Model structures for a copper (I)- copper(II) redox couple in copper proteins: X-ray powder structure of bis(imidazole) copper (I) perchlorate and crystal structure of bis(imidazole)copper(II) di- acetate. J. Chem. Soc. Chem. Comm. 130–131 (1976)

    Google Scholar 

  • Jolley, R.L., Evans, L.H., Makino, N., Mason, H.S.: Oxytyrosinase. J. Biol. Chem. 249, 335–345 (1974)

    PubMed  CAS  Google Scholar 

  • Klotz, I.M., Klippenstein, G.L., Hendrickson, W.A.: Hemerythrin: Alternative oxygen carrier. Science 192, 335–344 (1976)

    Article  PubMed  CAS  Google Scholar 

  • Klotz, I.M., Klotz, T.A.: Oxygen-carrying proteins: A comparison of the oxygenation reaction in hemocyanin and hemerythrin with that in hemoglobin. Science 121, 477– 480 (1955)

    Article  PubMed  CAS  Google Scholar 

  • Kobert, R. : Über Hemocyanin nebst einigen Notizen über Hamerythrin. Pflüger’s Arch. Physiol. 98, 411–427 (1903)

    Article  CAS  Google Scholar 

  • Kubowitz, F.: Spaltung und Resynthese der Polyphenoloxydase und des Hamocyanins. Biochem. Z. 299, 32–57 (1938)

    CAS  Google Scholar 

  • Lichtenberger, F., Nastainczyk, W., Ullrich, V.: Cytochrome P450 as an oxene transferase. Biochem. Biophys. Res. Comm. 70, 939–946 (1976)

    Article  PubMed  CAS  Google Scholar 

  • Lontie, R., Vanquickenborne, L.: The role of copper in hemocyanins. In: Metal Ions in Biological Systems. Vol. III. High Molecular Complexes. Sigel, H. (ed.). New York: Marcel Dekker, 1974, pp. 183–200

    Google Scholar 

  • Margerum, D.W., Chellappa, K.L., Bossu, F.P., Burce, G.L.: Characterization of a readily accessible copper(III)-peptide complex. J. Am. Chem. Soc. 97, 6894–6896 (1975)

    Article  PubMed  CAS  Google Scholar 

  • Moss, T.H., Gould, D.C., Ehrenberg, A., Loehr, J.S., Mason, H.S.: Magnetic properties of Cancer magister hemocyanin. Biochemistry 12, 2444–2449 (1973)

    Article  PubMed  CAS  Google Scholar 

  • Quagliariello, G.: Das Hamocyanin. Naturwissenschaften 11, 261–268 (1923)

    Article  CAS  Google Scholar 

  • Rabuteau, Papillon, F.: Observations sur quelques liquides de l’organisme des Pois- sons, des Crustaces et des Cephalopodes. C. R. Acad. Sci. (Paris) 77, 135–138 (1873)

    Google Scholar 

  • Redfield, A.C.: The haemocyanins. Biol. Rev. 9, 175–212 (1934)

    Article  CAS  Google Scholar 

  • Redfield, A.C., Coolidge, T., Montgomery, H.: The respiratory proteins of the blood. II. The copper-combining ratio of oxygen and copper in some bloods containing hemocyanin. J. Biol. Chem. 76, 197–205 (1928)

    CAS  Google Scholar 

  • Richardson, J.S., Thomas, K.A., Rubin, B.H., Richardson, D.C.: Crystal structure of bovine Cu,Zn superoxide dismutase at 3 A resolution: Chain tracing and metal li- gands. Proc. Natl. Acad. Sci. 72, 1349–1353 (1975)

    Article  PubMed  CAS  Google Scholar 

  • Roche, J., Dubouloz, P.: Etude de la constitution des hemocyanines et des hemery- thrines au moyen de leur spectre ultraviolet. C. R. Acad. Sci. (Paris) 196, 646 (1933)

    CAS  Google Scholar 

  • Salvato, B., Zatta, P., Ghiretti-Magaldi, A., Ghiretti, F.: On the active site of hemocyanin. FEBS Lett. _32, 35–36 (1973)

    Article  PubMed  CAS  Google Scholar 

  • Solomon, E.I., Dooley, D.M., Wang, R.H., Gray, H.B., Cerdonio, M., Mogno, F., Romani, G.L.: Susceptibility studies of laccase and oxyhemocyanin using an ultrasensitive magnetometer. Antiferrognetic behaviour of the type 3 copper in Rhus laccase. J. Am. Chem. Soc. 98, 1029–1031 (1976)

    Article  PubMed  CAS  Google Scholar 

  • Swammerdam, J.: Historia Insectorum Generalis ofte algemene verhandeling van de bloedeloose dierkens. Utrecht: van Dreunen, 1669

    Google Scholar 

  • Vaska, L.: Dioxygen-metal complexes: Toward a unified view. Accounts Chem. Res. 9, 175–183 (1976)

    Article  CAS  Google Scholar 

  • Witters, R., Goyffon, M., Lontie, R.: Etude de 1’hemocyanine de Scorpion par dichro- isme circulaire. C. R. Acad. Sci. (Paris) _278, 1277–1280 (1974)

    CAS  Google Scholar 

  • Witters, R., Lontie, R.: The formation of Helix pomatia methaemocyanin accelerated by azide and fluoride. FEBS Lett. 60, 400-403 (1975)

    Article  PubMed  CAS  Google Scholar 

Download references

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1977 Springer-Verlag Berlin Heidelberg

About this paper

Cite this paper

Lontie, R. (1977). On the Active Site of Molluscan Haemocyanin and of Tyrosinases. Opening Address. In: Bannister, J.V. (eds) Structure and Function of Haemocyanin. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-66679-7_19

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-66679-7_19

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-66681-0

  • Online ISBN: 978-3-642-66679-7

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics