The features of Mössbauer spectra of hemoglobin in relation to the quadrupole splitting and heme iron stereochemistry

Zeitschrift fur Naturforschung - Section A Journal of Physical Sciences

Volumn 53, Issue 6-7, 1998, Pages 608-614

  Oshtrakh, M I ^a  

^a URAL FEDERAL UNIVERSITY   (Russian Federation)

Author keywords

Heme Iron Stereochemistry; Human Hemoglobins; M ssbauer Spectroscopy; Quadrupole Splitting

Indexed keywords

EID: 0039398570     PISSN: 09320784     EISSN: None     Source Type: Journal    
DOI: 10.1515/zna-1998-6-755     Document Type: Article

References (34)

1. J.M. Baldwin, Prog. Biophys. Molec. Biol. 29, 225 (1975).
2. M. F. Perutz, Ann. Rev. Biochem. 48, 327 (1979).
3. U. Gonser, R. W. Grant, and J. Kregzde, Appl. Phys. Lett. 3, 189 (1963).
4. U. Gonser and R. W. Grant, Biophys. J. 5, 823 (1965).
5. G. Lang and W. Marshall, Proc. Phys. Soc. 87, 3 (1966).
6. A. Vertes, L. Korecz, and K. Berger, Mössbauer Spectroscopy, Academia Kiada, Budapest 1979, p. 344.
7. K. Spartalian and G. Lang, in: Applications of Mössbauer Spectroscopy, Vol. II, Academic Press, Inc., New York 1980, p. 249.
8. A. Trautwein and E. Bill, in: Transition Met. Chem., Proc. Workshop 1980, Verlag Chemie 1981, p. 239.
9. D. P. E. Dickson, in: Mössbauer Spectroscopy Applied to Inorganic Chemistry, ed. G. J. Long, Vol. 1, Plenum, New York 1984, p. 339.
10. M. I. Oshtrakh, Hyperfine Interact. 66, 127 (1991).
11. M. I. Oshtrakh, Z. Naturforsch. 51a, 381 (1996).
12. M.I. Oshtrakh and V.A. Semionkin, Mol. Biol. Moscow 19, 1310 (1985).
13. B.N. Burykin, V.A. Khleskov, M.I. Oshtrakh, and V. A. Semionkin, Mol. Biol. Moscow 21, 1677 (1987).
14. M. I. Oshtrakh and V. A. Semionkin, FEBS Lett. 208, 331 (1986).
15. M.I. Oshtrakh and V. A. Semionkin, FEBS Lett. 257, 41 (1989).
16. M. I. Oshtrakh, J. Inorg. Biochem. 56, 221 (1994).
17. E. R. Bauminger and S. Ofer, Proc. Ind. Natl. Sci. Academy, Proc. Int. Conf. Appl. Mössbauer Effect, New Delhi 1982, p. 61.
18. M.I. Oshtrakh and V.A. Semionkin, Biophysica Moscow 28, 135 (1983).
19. L. Cianchi, F. Pieralli, F. Del Giallo, M. Mancini, G. Spina, and L. Fiesoli, Phys. Lett. 100A, 57 (1984).
20. B. Boso, P.G. Debrunner, G.C. Wagner, and T. Inubushi, Biochim Biophys Acta 791, 244 (1984).
21. G. R. Hoy, D. C. Cook, R. L. Berger, and F. K. Friedman, Biophys. J. 49, 1009 (1986).
22. V. E. Prusakov, R. A. Stukan, and V. I. Goldanskii, Biomed. Sci. 2, 127 (1991).
23. J. A. Frier and M. F. Perutz, J. Mol. Biol. 112, 97 (1977).
24. A. Bianconi, A. Congiu-Castellano, M. Dell'Ariccia, A. Giovannelli, E. Burattini, M. Castagnola, and P.J. Durham, Biochim. Biophys. Acta 831, 120 (1985).
25. E. Bill, E. Di Iorio, A. Trautwein, and K. Winterhalter, Proc. Ind. Natl. Sci. Academy, Proc. Int. Conf. Appl. Mössbauer Effect, New Delhi 1982, p. 648.
26. M. F. Perutz, G. Fermi, B. Luisi, B. Shaanan, and R. C. Liddington, Acc. Chem. Res. 20, 309 (1987).
27. B. Shaanan, J. Mol. Biol. 171, 31 (1983).
28. J. S. Olson, A. J. Mathews, R. J. Rohlfs, B. A. Springer, K. D. Egelberg, S. G. Sugar, J. Tame, J.-P. Renaud, and K. Nagai, Nature London 336, 265 (1988).
29. Z. S. Herman and G. H. Loew, J. Amer. Chem. Soc. 102, 1815 (1980).
30. R. F. Kirchner and G. H. Loew, J. Amer. Chem. Soc. 99, 4639 (1977).
31. W. R. Scheldt and C. A. Reed, Chem. Rev. 81, 543 (1981).
32. L. Pauling, Nature London 203, 182 (1964).
33. W. A. Goddard, III and B. D. Olafson, Proc. Natl. Acad. Sci. USA 72, 2335 (1975).
34. V. A. Khleskov, B. N. Burykin, A.B. Smirnov, and M. I. Oshtrakh, Biochem. Biophys. Res. Communs. 155, 1255 (1988).