Skip to main content
SpringerLink
Log in

ESR and optical absorption studies on the copper(II) interaction with small peptides containing aromatic amino acids

  • Published:
Biophysics of structure and mechanism Aims and scope Submit manuscript

Abstract

The interaction of Cu(II) with di- and tripeptides each containing phenylalanine, tryptophan or histidine in the amino acid chain has been investigated by means of electron spin resonance (ESR) and optical absorption spectroscopy. Cu(II) complexes of dipeptides and tripeptides exhibit different magnetic and optical parameters. Dipeptide complexes have larger g ∥-values and smaller {A ∥−values than tripeptide complexes. When compared to dipeptide complexes, the d-d band of the central metal ion is blue shifted for tripeptide complexes. There are no significant differences in the behavior of Cu(II) peptide complexes containing phenylalanine or tryptophan. Complexes of histidine containing peptides, however, show modified spectra caused by the participation of the imidazole nitrogen in the coordination to Cu(II). The imidazole nitrogen seems to coordinate in-plane with other coordinating atoms or in an axial position depending on the kind of peptide.

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. Boas, J. F., Pilbrow, J. R., Hartzell, C. R., Smith, T. D.: Electron spin resonance studies of some copper(II) peptide complexes. J. Chem. Soc. (A) 572–577 (1969)

  2. Bryce, F. G.: Electron paramagnetic resonance study of cupric-peptide complexes. J. Phys. Chem. 70, 3549–3557 (1966)

    Google Scholar 

  3. Bryce, G. F., Gurd, F. R. N.: Visible spectra and optical rotatory properties of cupric ion complexes of l-histidine containing peptides. J. Biol. Chem. 241, 122–129 (1966)

    Google Scholar 

  4. Falk, K. E., Freeman, H. C., Jansson, T., Malmström, B. G., VÄnngard, T.: Magnetic resonance studies of copper(II)-triglycylglycine complexes. J. Amer. Chem. Soc. 89, 6071–6077 (1967)

    Google Scholar 

  5. Finazzi-AgrÒ, A., Rotilio, G., Avigliano, L., Guerrieri, P., Boffi, V., Mondoví, B.: Environment of copper in pseudomonas fluorescens azurin: Fluorometric approach. Biochemistry 9, 2009–2014 (1970)

    Google Scholar 

  6. Freeman, H. C.: Crystal structure studies of cupric-peptide complexes. In: Biochemistry of copper (eds. J. Peisach, P. Aisen, W. E. Blumberg), pp. 77–113. New York-London: Academic Press 1966

    Google Scholar 

  7. Gersmann, H. R., Swalen, J. D.: Electron paramagnetic resonance spectra of copper complexes. J. Chem. Phys. 36, 3221–3233 (1962)

    Google Scholar 

  8. Giordano, R. S., Bereman, R. D.: Stereoelectronic properties of metallo enzymes. I. A. comparison of the coordination of copper(II) in galactose oxidase and a model system, N,N′-ethylenebis(trifluoroacetylacetoniminato) copper(II). J. Amer. Chem. Soc. 96, 1019–1023 (1974)

    Google Scholar 

  9. Kim, M. K., Martell, A. E.: Copper(II) complexes of glycylglycine. Biochemistry 3, 1169–1174 (1964)

    Google Scholar 

  10. Kivelson, D., Neiman, R.: ESR studies on the bonding in copper complexes. J. Chem. Phys. 35, 149–155 (1961)

    Google Scholar 

  11. Kruck, Th. P. A., Sarkar, B.: Equilibria and structure of the species in the ternary system of l- histidine, copper(II), and diglycyl-l-histidine, a peptide mimicking the copper(II)-transport site of human serum albumin. Inorg. Chemistry 14, 2383–2388 (1975)

    Google Scholar 

  12. Lau Show-Jy, Kruck, Th. P. A., Sarkar, B.: A peptide molecule mimicking the copper(II) transport site of human serum albumin. J. Biol. Chem. 249, 5878–5884 (1974)

    Google Scholar 

  13. Llinás, M.: Metal-polypeptide interactions: The conformational state of iron proteins. In: Structure and bonding, vol. 17 (eds. J. D. Dunitz, P. Hemmerich, R. H. Holm, J. A. Ibers, C. K. JØrgensen, J. B. Neilands, D. Reinen, R. J. P. Williams), pp. 135–220. Berlin-Heidelberg-New York: Springer 1973

    Google Scholar 

  14. Margerum, D. W., Chellappa, K. L., Bossu, F. P., Gary, L. B.: Characterization of a readly accessible copper(III)-peptide complex. J. Amer. Chem. Soc. 97, 6894–6896 (1975)

    Google Scholar 

  15. McGarvey, B. R.: Electron spin resonance of transition-metal complexes. In: Transition metal chemistry, vol. 3 (ed. R. L. Calvin), pp. 89–201. New York-London: Dekker 1969

    Google Scholar 

  16. McMillin, D. R., Holwerda, R. A., Gray, H. B.: Preparation and spectroscopic studies of cobalt(II)-stellacyanin. Proc. Nat. Acad. Sci. USA 71, 1339–1341 (1974)

    Google Scholar 

  17. Meyer, J. L., Bauman, J. E., Jr.: Copper(II)-histidine complexes. J. Amer. Chem. Soc. 92, 4210–4216 (1970)

    Google Scholar 

  18. Ross, R. T.: Dipolar broadening in ESR spectra due to solute aggregation in frozen aqueous solutions. J. Chem. Phys. 42, 3915–3922 (1965)

    Google Scholar 

  19. Rotilio, G., Morpurgo, L., Calabrese, L., Finazzi-AgrÒ, A., Mondoví, B.: Metal-ligand interaction in Cu-enzymes. IX. Jerusalem Symposium on: Metal-ligand interaction in organic chemistry and biochemistry, Jerusalem, 29. 3.–2. 4. 1976

  20. Sheinblatt, M., Becker, E. D.: Spectrophotometric studies of Cu(II) complexes of glycylglycine. J. Biol. Chem. 242, 3159–3163 (1967)

    Google Scholar 

  21. Sportelli, L., Neubacher, H., Lohmann, W.: ESR and optical studies on the copper(II) interaction with aromatic amino acids. Rad. and Environm. Biophys. 13, 305–313 (1976)

    Google Scholar 

  22. Sugiura, Y., Hirayama, Y., Tanaka, H., Ishizu, K.: Copper(II) complex of sulfur-containing peptides. Characterization and similarity of electron spin resonance spectrum to the chromophore in blue copper proteins. J. Amer. Chem. Soc. 97, 5577–5581 (1975)

    Google Scholar 

  23. Urry, D. W., Eyring, H.: Optical rotatory dispersion studies of l-histidine chelation. J. Amer. Chem. Soc. 86, 4574–4580 (1964)

    Google Scholar 

  24. VÄnngard, T.: Copper proteins. In: Biological applications of electron spin resonance. (eds. H. M. Swartz, J. R. Bolton, D. C. Borg), pp. 411–447. New York: Wiley-Interscience 1972

    Google Scholar 

  25. Voelter, W., Sokolowski, G., Weber, U., Weser, U.: The initial binding of Cu(II) to some amino acids and dipeptides: A 13C nuclearmagnetic-resonance study. Europ. J. Biochem. 58, 159–166 (1975)

    Google Scholar 

  26. Wellmann, K. M., Wong, B. K.: Structure and optical activity in metal complexes. VI. Interaction of histidine with copper(II) in solution. Proc. Nat. Acad. Sci. USA 64, 824–827 (1969)

    Google Scholar 

  27. Yokoi, H., Isobe, T.: Molecular association of 1∶2 complexes of copper(II) with amino acids in aqueous media. Chemistry Lett. 95–98 (1972)

Download references

Author information

Authors and Affiliations

  1. Institut für Biophysik, Strahlenzentrum der Justus-Liebig-Universität Gie\en, Leihgesterner Weg 217, D-6300, Gie\en

    Luigi Sportelli, Harald Neubacher & Wolfgang Lohmann

  2. Abteilung für Biophysikalische Chemie, GSF, D-8042, Neuherberg, Federal Republic of Germany

    Luigi Sportelli, Harald Neubacher & Wolfgang Lohmann

Authors
  1. Luigi Sportelli
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Harald Neubacher
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Wolfgang Lohmann
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

Dedicated to Prof. Dr. H. Glubrecht on the occasion of his 60th birthday

Part of the Ph.D. thesis of L.S., D-26

Rights and permissions

Reprints and permissions

About this article

Cite this article

Sportelli, L., Neubacher, H. & Lohmann, W. ESR and optical absorption studies on the copper(II) interaction with small peptides containing aromatic amino acids. Biophys. Struct. Mechanism 3, 317–326 (1977). https://doi.org/10.1007/BF00535704

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00535704

Key words

Search

Navigation