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The iron–oxygen bond in human oxyhaemoglobin

Nature volume 296, pages 683684 (15 April 1982) | Download Citation

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Abstract

Knowledge of the exact nature of the iron–oxygen bond in oxyhaemoglobin (oxyHb) is essential for the understanding of cooperative oxygen binding to haemoglobin (Hb)1. However, X-ray studies of oxyHb have previously been hindered by the tendency of oxyHb crystals to autoxidize. Here we report the stereochemistry of the haem–oxygen complex in human oxyHb, as determined by single-crystal X-ray analysis. Bent end-on geometry of the iron–oxygen bond in haem proteins, as predicted by Pauling2, was first observed in the ‘picket fence’ complex3 and has since been observed in oxymyoglobin (oxyMb)4,5; in oxyerythrocruorin, however, the Fe—O—O bond is almost linear6. In oxyHb the Fe—O—O bond angle is 156°, intermediate between the ‘picket fence’ compound and erythrocruorin. The position of Nɛ of His E7 in the α-subunit suggests that it forms a hydrogen bond with the bound oxygen, as in oxyMb7. In the β-subunit, however, Nɛ of His E7 is located further from the oxygen, suggesting that the hydrogen bond is weaker.

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References

  1. 1.

    A. Rev. Biochem. 48, 327–386 (1979).

  2. 2.

    Nature 203, 182–183 (1964).

  3. 3.

    , , , & Proc. natn. Acad. Sci. U.S.A. 71, 1326–1329 (1974).

  4. 4.

    Nature 273, 247–248 (1978).

  5. 5.

    J. molec. Biol. 142, 531–554 (1980).

  6. 6.

    & J. molec. Biol. 127, 309–338 (1979).

  7. 7.

    & Nature 292, 81–82 (1981).

  8. 8.

    J. Crystal Growth 2, 54–56 (1968).

  9. 9.

    , , & J. appl. Crystallogr. 6, 457–463 (1973).

  10. 10.

    J. molec. Biol. 136, 103–128 (1980).

  11. 11.

    & Acta crystallogr. A34, 782–791 (1978).

  12. 12.

    Acta crystallogr. 5, 802–810 (1952).

  13. 13.

    , & Inorg. Chem. 16, 503–511 (1977).

  14. 14.

    & J. Am. chem. Soc. 99, 4639–4647 (1977).

  15. 15.

    Br. med. Bull. 32, 195–208 (1976).

  16. 16.

    , , , & J. Am. chem. Soc. 103, 2450–2452 (1981).

  17. 17.

    & Biochemistry 12, 4946–4949 (1973).

  18. 18.

    & J. biol. Chem. 254, 4532–4535 (1979).

  19. 19.

    et al. J. Am. chem. Soc. 102, 3224–3237 (1980).

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Affiliations

  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK

    • Boaz Shaanan

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DOI

https://doi.org/10.1038/296683a0

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