Skip to main content
Log in

Does cobalt really bind tightly to hemocyanin active sites?

  • Published:
European Biophysics Journal Aims and scope Submit manuscript

Abstract

The analysis of Co(II)-apoHc complexes of two arthropodan species (freshwater crayfish): Orconectes limosus and Astacus astacus enabled to reach some conclusions about possible cobalt binding sites in the hemocyanin molecules. The occurrence of binding sites for Co(II) at sites other than the active center has been demonstrated. We excluded the possibility of strong binding of EDTA-non-removable cobalt ions in the binding sites occupied by copper. There were no differences between apoHc and the Co(II)apoHc complex in terms of the amount of bound Cu(I) ions and the kinetics of Cu(I) ion reconstitution.

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

Access this article

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

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

He:

hemocyanin

apoHc:

apohemocyanin

oxyHc:

oxyhemocyanin

Co-Hc:

hemocyanin complex with cobalt ions

References

  • Belleli A, Zolla L, Giordani B, Costantini S, Cau A, Brunori M (1985) Hemocyanin from Palinurus elephas: general properties and effect of heavy metals. Biochim Biophys Acta 830: 325–331

    Google Scholar 

  • Brouwer M, Engel DW (1982) Stoichiometry and functional consequences of Hg(II) and Cd(II) binding to arthropod hemocyanins. In: Physiological mechanism of marine pollutant toxicity. Academic Press, New York, pp 289–310

    Google Scholar 

  • Gondko R, Michalak W (1981) Some physicochemical properties of hemocyanin of crayfish. In: Lamy J, Lamy J (eds) Invertebrate oxygen-binding proteins. Dekker, New York, pp 41–47

    Google Scholar 

  • Gondko R, Serafin E, Mazur J, Jeowska-Trzebiatowska B, Jezierski A (1985) The kinetics of the reaction of thiocyanate and nitrite ions with Orconectes limosus oxyhemocyanin. Z Naturforsch 40c: 44–48

    Google Scholar 

  • Himmelwright RS, Eickman NC, Lu Bien CD, Solomon EI (1980) Chemical and spectroscopic comparison of the binuclear copper active site of mollusc and arthropod hemocyanins. J Am Chem Soc 102: 5378–5388

    Google Scholar 

  • Jones RD, Summervile DA, Bosolo F (979) Synthetic oxygen carriers related to biological systems. Chem Rev 79: 139–179

    Google Scholar 

  • Konings WN, Van Driel R, Van Bruggen EFJ, Gruber M (1969) Structure and properties of hemocyanins. V. Binding of oxygen and copper in Helix pomatia hemocyanin. Biochim Biophys Acta 194: 55–60

    Google Scholar 

  • Lorosch J, Haase J (1986) Cobalt(II)-Hemocyanin: Model for the cuprous deoxy protein giving evidence for a bridging ligand in the active site. Biochemistry 25: 5850–5857

    Google Scholar 

  • Salvato B, Beltramini M, Piazzesi A, Alvigi M, Ricchelli F (1986) Preparation, spectroscopic characterization and anion binding studies of a mononuclear Co(H) derivative of Carcinus maenas hemocyanin. Inorg Chim Acta 125: 55–62

    Google Scholar 

  • Suzuki S, Kino J, Kimura M, Mori N, Nakahara A (1982a) Structure of the active site of hemocyanin. Cobalt (II)-substituted squid hemocyanin. Inorg Chim Acta 66: 41–47

    Google Scholar 

  • Suzuki S, Kino J, Nakahara A (1982b) Cobalt(II)-substituted horseshoe crab hemocyanins. Bull Chem Soc Jpn 55: 212–217

    Google Scholar 

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

    Google Scholar 

  • Witters R, Lontie R (1983) Characterization of cobalt-substituted haemocyanin of Helix pomatia. Life Chem Rep [Suppl] 1: 285–288

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

Offprint requests to: E. Serafln

Rights and permissions

Reprints and permissions

About this article

Cite this article

Serafin, E., Gondko, R. Does cobalt really bind tightly to hemocyanin active sites?. Eur Biophys J 18, 117–120 (1990). https://doi.org/10.1007/BF00183270

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00183270

Key words

Navigation