Stereochemistry of iron in deoxyhaemoglobin (original) (raw)

Nature volume 295, pages 535–538 (1982)Cite this article

Abstract

X-ray crystallography has shown that in deoxyhaemoglobin the iron atoms are displaced by 0.56±0.03 Å from the mean porphyrin plane, whereas in liganded haemoglobins they lie either in or close to that plane1,2. Perutz3 proposed this shift as one principal factor responsible for haem–haem interaction. Eisenberger et al. used extended X-ray absorption fine structure (EXAFS) to measure the Fe–N distance in deoxyhaemoglobin and concluded that the irons lie only 0.2+0.1−0.2 Å from the plane of the porphyrin nitrogens and that the mechanism of Perutz is therefore invalid4. We have now compared the EXAFS of deoxyhaemoglobin with that of the ferrous ‘picket fence’ 2-methylimidazole complex in which the displacement of the iron from the plane of the porphyrin nitrogens is known to be 0.399±0.004 and 0.426±0.004 Å from the mean porphyrin plane (ref. 5). The two EXAFS spectra are very similar, consistent with similar displacements of the irons. We find the same Fe–N distance of 2.06±0.01 Å in deoxyhaemoglobin as Eisenberger et al., but show that the displacement of the iron cannot be calculated from that distance.

This is a preview of subscription content, access via your institution

Access options

Subscribe to this journal

Receive 51 print issues and online access

$199.00 per year

only $3.90 per issue

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Additional access options:

Similar content being viewed by others

References

  1. Fermi, G., Perutz, M. F., Dickinson, L. C. & Chien, J. C. W. J. molec. Biol. (in the press).
  2. Perutz, M. F. A. Rev. Biochem. 48, 327–386 (1979).
    Article CAS Google Scholar
  3. Perutz, M. F. Nature 228, 726–739 (1970).
    Article ADS CAS Google Scholar
  4. Eisenberger, P., Shulman, R. G., Kincaid, B. M., Brown, G. S. & Ogawa, S. Nature 274, 30–34 (1978).
    Article ADS CAS Google Scholar
  5. Jameson, G. B. et al. J. Am. chem. Soc. 102, 3224–3237 (1980).
    Article CAS Google Scholar
  6. Bordas, J., Bray, R. C., Garner, C. D., Gutteridge, S. & Hasnain, S. S. Biochem. J. 191, 499–508 (1980).
    Article CAS Google Scholar
  7. Hasnain, S. S. et al. J. Am. chem. Soc. (submitted).
  8. Lee, P. A. & Pendry, J. B. Phys. Rev. 11B, 2795 (1975).
  9. Pendry, J. B. in EXAFS for Inorganic Systems (eds Garner, C. D. & Hasnain, S. S.) 5 (Proc. Daresbury Study Weekend, 1981).
    Google Scholar
  10. Fermi, G. J. molec. Biol. 114, 412–413 (1977).
    Google Scholar
  11. Jameson, G. B., Robinson, W. T., Collman, J. P. & Sorrell, T. N. Inorg. Chem. 17, 858–864 (1978).
    Article CAS Google Scholar
  12. Greaves, G. N., Durham, P. J., Deakun, D. P. & Quinn, P. D. Nature 294, 139–142 (1981).
    Article ADS CAS Google Scholar
  13. Warshel, A. Proc. natn. Acad. Sci. U.S.A. 74, 1789–1793 (1977).
    Article ADS CAS Google Scholar
  14. Hopfield, J. J. J. molec. Biol. 77, 202–222 (1973).
    Article Google Scholar
  15. Hoard, J. L. in Porphyrins and Metalloporphyrins (ed. Smith, K. M.) 318–380 (Elsevier, Amsterdam, 1975).
    Google Scholar

Download references

Author information

Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Cambridge, CB2 2QH, UK
    M. F. Perutz
  2. Daresbury Laboratory, Warrington, WA4 4AD, UK
    S. Samar Hasnain & P. J. Duke
  3. Department of Chemistry, Stanford University, Stanford, California, 94305, USA
    J. L. Sessler & J. E. Hahn

Authors

  1. M. F. Perutz
    You can also search for this author inPubMed Google Scholar
  2. S. Samar Hasnain
    You can also search for this author inPubMed Google Scholar
  3. P. J. Duke
    You can also search for this author inPubMed Google Scholar
  4. J. L. Sessler
    You can also search for this author inPubMed Google Scholar
  5. J. E. Hahn
    You can also search for this author inPubMed Google Scholar

Rights and permissions

About this article

Cite this article

Perutz, M., Hasnain, S., Duke, P. et al. Stereochemistry of iron in deoxyhaemoglobin.Nature 295, 535–538 (1982). https://doi.org/10.1038/295535a0

Download citation

This article is cited by