Skip to main content
SpringerLink
Log in

Investigation of the electronic term scheme of deoxygenated human haemoglobin by a least squares fit procedure using simultaneously magnetic susceptibility and Mössbauer data

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

Summary

The calculation of the magnetic susceptibility from a published term scheme for the ferrous iron in deoxygenated human haemoglobin is discussed and a procedure for the simultaneous least squares fit of susceptibility and Mössbauer data is presented. The application of this procedure to the appropriate measurements on human haemoglobin leads to a rearrangement of the low lying electronic levels of the iron. The term schemes received as results of two different sets of susceptibility data used in combination with one set of Mössbauer data overlap with their error bars. The obtained level scheme of the Fe is correlated with the distance of the iron atom from the haem plane and the distance Fe-HIS F8, and some biological implications of these correlations are discussed.

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

  • Alpert, Y., Banerjee, R.: Magnetic susceptibility measurements of deoxygenated hemoglobins and isolated chains. Biochim. biophys. Acta (Amst.) 405, 144–154 (1975)

    Google Scholar 

  • Antonini, E., Wyman, J., Rossi Fanelli, A., Caputo, A.: Studies on the relations between molecular and functional properties of haemoglobin(III). J. biol. Chem. 237, 2773–2777 (1962)

    Google Scholar 

  • Bade, D., Parak, F., Thomanek, U. F., Kalvius, G. M.: Mössbauer effect and magnetic susceptibility investigations of human haemoglobin. Proceedings of the International Conference on Mössbauer Spectroscopy, Cracow, vol. 1, 439–440 (1975)

    Google Scholar 

  • Braunitzer, G., Buse, G., Gersonde, K.: Structure and function of haemoglobins, from: Molecular oxygen in biology. Topics in molecular oxygen research, (ed. O. Hayaiski), Chapt. 6, pp. 183–218. Amsterdam: North Holland Publ. 1974

    Google Scholar 

  • Davydow, A. S.: Quantum mechanics. London: Pergamon Press 1965

    Google Scholar 

  • Eicher, H., Trautwein, A.: Electronic structure and quadrupole splittings of ferrous iron in haemoglobin. J. chem. Phys. 50, 2540–2551 (1969)

    Google Scholar 

  • Eicher, H., Trautwein, A.: Electronic structure of ferrous iron in haemoglobin inferred from Mössbauer measurements. J. chem. Phys. 52, 932–934 (1970)

    Google Scholar 

  • Eicher, H., Parak, F., Bade, D., Tejada, J.: Electronic structure of the iron in deoxygenated myoglobin from Mössbauer spectroscopy. J. Phys. (Paris) 35, C6, 363–366 (1974)

    Google Scholar 

  • Eicher, H., Bade, D., Parak, F.: Theoretical determination of the electronic structure and the spatial arrangement of the ferrous iron in deoxigenated sperm whale myoglobin and human haemoglobin from Mössbauer spectroscopy. J. Phys. (Paris) 35, C6, 363–366 (1974)

    Google Scholar 

  • Huynh, B. H., Papaefthymiou, G. C., Yen, C. S., Groves, J. L., Wu, C. S.: Electronic structure of Fe2+ in normal human haemoglobin and its isolated subunits. J. chem. Phys. 61, 3750–3758 (1974)

    Google Scholar 

  • Marquardt, D. W.: An algorithm for least squares estimation of nonlinear parameters. J. Soc. Ind. Appl. Math. 11, 431–441 (1963)

    Google Scholar 

  • Nakano, N., Otsuka, J., Tasaki, A.: Fine structure of iron in deoxymyoglobin and deoxyhaemoglobin. Biochim. biophys. Acta (Amst.) 236, 222–233 (1971)

    Google Scholar 

  • Perutz, M. F.: Stereochemistry of cooperative effects in haemoglobin. Nature (Lond.) 228, 726–739 (1970)

    Google Scholar 

  • Perutz, M. F., Ladner, J. E., Simon, S. R., Ho, C.: Influence of globin structure on the state of the heme. 1. Human deoxyhaemoglobin. Biochemistry 13, 2163–2173 (1974)

    Google Scholar 

  • Perutz, M. F., Fersht, A. R., Simon, S. R., Roberts, G. C. K.: Influence of globin structure on the state of the heme. 2. Allosteric transitions in methemoglobin. Biochemistry 13, 2174–2186 (1974)

    Google Scholar 

  • Perutz, M. F., Heidner, E. J., Ladner, J. E., Beetlestone, J. G., Ho, C.: Influence of the globin structure on the state of the heme. 3. Changes in heme spectra accompanying allosteric transitions in methemoglobin and their implications for heme — heme interaction. Biochemistry 13, 2187–2199 (1974)

    Google Scholar 

  • Perutz, M. F.: Priv. communication (1975)

  • Thomanek, U. F., Parak, F., Kalvius, G. M.: To be published (1976)

  • Zimmermann, R.: Properties of a 5T2 iron (II) under the action of arbitrary-symmetry ligand fields and spin orbit coupling. Phys. stat. sol. (b) 68, 181–191 (1975)

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Physikdepartment E 15 der Technischen UniversitÄt München, James-Franck-Straêe, D-8046, Garching, Federal Republic of Germany

    D. Bade & F. Parak

Authors
  1. D. Bade
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. F. Parak
    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

Bade, D., Parak, F. Investigation of the electronic term scheme of deoxygenated human haemoglobin by a least squares fit procedure using simultaneously magnetic susceptibility and Mössbauer data. Biophys. Struct. Mechanism 2, 219–231 (1976). https://doi.org/10.1007/BF00535368

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00535368

Key words

Search

Navigation