Journal of Structural Chemistry

, Volume 34, Issue 5, pp 731–734 | Cite as

Influence of heme periphery on the electronic structure and Mössbauer parameters of hemoglobin

  • A. A. Karpov
  • V. I. Khleskov
  • A. B. Smirnov


For the five-coordinated complexes of ferroprotoporphynynn with imidazole, a quantum-chemical analysis of the electronic structure and Mossbauer spectral parameters has been canied out. Peripheral substituents (―CH3, ―Cf13, ―C2H4COOH) were introduced into the porphynin macrocycle to model the real chemical structure of protopo'phynynn in the heme group of desoxyhemoglobin. The calculations have shown that near the occupation border in the complaes there are MO which are due to the π-systems of the ―CH= CM2 and ―CH2―CH2COOH substituents. The orientalion of the vinyl fragments has a considerable effect on the populations of the Fe d-orbitals and the quadrupole splitting ΔEQ for the5B1 and5B2 terns.


Physical Chemistry Inorganic Chemistry Vinyl Imidazole Spectral Parameter 
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  1. 1.
    G. Braunitzer, K. Hilse, V. Rudloff, and N. Hilchmann,Adv. Protein Chem.,19, 1–71 (1964).Google Scholar
  2. 2.
    A. Rossi-Fanelli, E. Antonini, and A. Caputo,Adv. Protein Chem.,19, 74–222 (1964).Google Scholar
  3. 3.
    J. L. Hoard, in:Porphyrins and Metalloporphyrins., K. M. Smith (ed.), Elsevier, Amsterdam (1975), Chap. 8.Google Scholar
  4. 4.
    V. I. Khleskov, B. N. Burykin, A. B. Smirnov, and M. I. Oshtrakh,Biophys. Biochem. Res. Comm.,155, No. 3, 1255–1260 (1988).Google Scholar
  5. 5.
    B. N. Burykin, V. I. Khleskov, M. I. Oshtrakh, and V. A. Semenkin,Mol. Biol.,21, No. 6, 1677–1685 (1987).Google Scholar
  6. 6.
    M. I. Oshtrakh, V. A. Semionkin, B. N. Burykin, and V. I. Khleskov,Mol. Phys.,66, No. 2, 531–535 (1989).Google Scholar
  7. 7.
    G. Fermi, M. F. Perutz, B. Shaanan, and R. Fourme,J. Mol. Biol.,175, 159–174 (1984).Google Scholar
  8. 8.
    V. I. Khleskov and K. A. Konkov, Paper filed at VINITI, No. 2757-82, June 2, 1982, pp. 1–47.Google Scholar
  9. 9.
    V. I. Khleskov,Zh. Struk. Khim.,27, 172–173 (1986).Google Scholar
  10. 10.
    B. N. Burykin and V. I. Khleskov,Zh. Fiz. Khim.,63, No. 9, 2463–2467 (1989).Google Scholar
  11. 11.
    A. B. Smirnov and V. I. Khleskov,Teor. Éksp. Khim.,25, 601–606 (1989).Google Scholar
  12. 12.
    V. I. Khleskov, A. B. Smirnov, and R. E. Garibiv,Koordinats. Khim.,15, 308–315 (1989).Google Scholar
  13. 13.
    V. I. Khleskov, B. N. Burykin and A. B. Smirnov,Zh. Struk. Khim.,30, 148–162 (1989).Google Scholar
  14. 14.
    B. N. Burykin and V. I. Khleskov, Paper filed at VINITI, No. 1799-B86, March 17, 1986, pp. 1–45.Google Scholar
  15. 15.
    B. N. Burykin, Physical and Mathematical Sciences Candidate's Dissertation, Institute of Biophysics, Ministry of Health, Russian Federation, Moscow (1987).Google Scholar
  16. 16.
    B. N. Burykin and V. I. Khleskov,Teor. Éksp. Khim.,23, 506–508 (1987).Google Scholar
  17. 17.
    A. Trautwein, Y. Alpert, Y. Maeda, et al.,J. Phys. Coloque C6,37, 191–210 (1976)Google Scholar

Copyright information

© Plenum Publishing Corporation 1994

Authors and Affiliations

  • A. A. Karpov
  • V. I. Khleskov
  • A. B. Smirnov

There are no affiliations available

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