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

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Abstract

Electron spin resonance and optical absorption studies have been done in order to investigate the interaction between Cu2+ and aromatic amino acids in aqueous solution at 77 K and at room temperature as well. Depending on the concentration each aromatic amino acid can form two different kinds of complexes with Cu2+ which can be characterized by its ESR pattern. Additional information was obtained from optical d-d and CT transitions.

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References

  1. Allen, H. C., Jr., Mandrioli, M. I., Becker, J. W.: EPR spectra of some copper (II)-amino acid complexes. J. Chem. Phys.56, 997–999 (1972)

    Google Scholar 

  2. Bleany, B., Bowers, K. B.: Anomalous paramagnetism of copper acetate. Proc. Roy. Soc. (Lond.)A214, 451–465 (1952)

    Google Scholar 

  3. Boas, J. F., Pilrow, J. R., Smith, T. D.: An electron spin resonance study of dimer formation of copper (II) protoporphyrin. IX. J. Chem. Soc. (A) 1969, 721–723

  4. Boas, J. F., Pilrow, J. R., Smith, T. D.: Electron spin resonance studies of dimer formation by chelates of copper (II) with some amino acids. J. Chem. Soc. (A) 1969, 723–725

  5. Bryce, G. F.: Electron paramagnetic resonance study of cupric-peptide complexes. J. Phys. Chem.70, 3548–3557 (1966)

    Google Scholar 

  6. Cumpelik, O: Unpublished results

  7. 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 

  8. Fujimoto, M., Wylie, L. A., Saito, S.: Ligand hyperfine interaction in Cu2+ complexes in amino acid crystals: L-alanine-d4 andα-glycine-d2. J. Chem. Phys.58, 1273–1276 (1973)

    Google Scholar 

  9. Fujimoto, M., Tomkiewicz, Y.: ESR studies of copper-doped L-alanine crystals: Ultraviolet-induced conversion in Cu2+ complexes. J. Chem. Phys.56, 749–754 (1972)

    Google Scholar 

  10. Giordano, R. S., Bereman, R. D.: Stereoelectronic properties of metalloenzymes. 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, 1019–1026 (1973)

    Google Scholar 

  11. Kato, M., Jonasson, H. B., Fanning, J. C.: Copper (II) complexes with subnormal magnetic moments. Chem. Rev.64, 99–128 (1964)

    Google Scholar 

  12. Kroneck, P.: Models for the electron paramagnetic resonance non detectable copper in “blue oxidases”. A binuclear copper (II) complex with oxidized glutathione. J. Amer. Chem. Soc.97, 3839–3841 (1975)

    Google Scholar 

  13. Lohmann, W.: Charge-transfer interaction of aliphatic amino acids with metal ions. Z. Naturforsch.26b, 1098–1101 (1971)

    Google Scholar 

  14. Malmström, G., Vänngard, T.: Electron spin resonance of copper proteins and some model complexes. J. Mol. Biol.2, 118–124 (1960)

    Google Scholar 

  15. McConnel, H. M.: Effect of anisotropic hyperfine interaction on paramagnetic relaxation in liquids. J. Chem. Phys.25, 709–711 (1956)

    Google Scholar 

  16. Peisach, J., Aisen, P., Blumberg, W. E. (Eds.): Biochemistry of copper, New York-London: Academic Press 1966

    Google Scholar 

  17. Rist, G. H., Hyde, J. S., Vänngard, T.: Electron-nuclear double resonance of a protein that contains copper: Evidence for nitrogen coordination to Cu(II) in stellacyanin. Proc. Nat. Acad. Sci. (Wash.)67, 79–86 (1970)

    Google Scholar 

  18. Rosenberg, R. C., Root, C. A., Bernstein, P. K., Gray, H. B.: Spectral studies of copper (II) Carboxypeptidase A and related model complexes. J. Amer. Chem. Soc.97, 2092–2096 (1975)

    Google Scholar 

  19. Urry, P. W., Eyring, H.: Optical rotatory dispersion studies of L-histidine chelation. J. Amer. Chem. Soc.84, 4574–4580 (1964)

    Google Scholar 

  20. Vänngard, T.: Copper proteins. In: Biological applications of electron spin resonance, p. 411 (Swartz, H. M., Bolton, J. R., Borg, D. C.,Eds.). New York: Wiley-Interscience 1972

    Google Scholar 

  21. Windle, J. J., Wiersema, A. K., Clark, J. R., Feeney, R. E.: Investigation of the iron and copper complexes of avian conalbumins and human transferrins by electron paramagnetic resonance. Biochemistry2, 1341–1345 (1963)

    Google Scholar 

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

  23. Yokoi, H., Sai, M., Isobe, T., Oksawa, S.: ESR studies of the copper (II) complexes of amino acids. Bull. Chem. Soc. Japan45, 2189–2195 (1972)

    Google Scholar 

  24. Zuberbuhler, A., Mason, H. S.: An ESR study of Cu(II) L-cystinyl-bis-glycine. In: Magnetic resonance in biological systems, p. 187 (Ehrenberger, A., Malmström, B. G., Vänngard, T.,Eds.). Oxford-London-Edinburgh-New York-Toronto-Sydney-Paris-Braunschweig: Pergamon Press 1967

    Google Scholar 

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Sportelli, L., Neubacher, H. & Lohmann, W. ESR and optical absorption studies on the copper (II) interaction with aromatic amino acids. Radiat Environ Biophys 13, 305–313 (1976). https://doi.org/10.1007/BF01331175

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