Letter | Published:

Structure of oxymyoglobin

Abstract

MYOGLOBIN (Mb) consists of a single polypeptide chain of 153 residues and one haem. It combines reversibly with molecular oxygen which it takes up from the blood and passes on to mitochondria in muscle. In vivo its iron atom remains ferrous, but in vitro it autoxidises to the ferric metmyoglobin (metmb) in which the sixth ligand at the iron is water. Metmb of sperm whale was the first protein structure to be determined1. Takano recently determined the closely related structure of deoxymb by X-ray analysis, while that of COmb has been determined by neutron diffraction (refs 2, 3 and B. P. Schoenborn, personal communication). The most interesting structure, that of oxymb, has proved elusive. Watson and Nobbs tried to determine it by rapid crystallisation and collection of X-ray data at 4 °C, but even so autoxidation obscured the results4. Recent advances in low temperature techniques encouraged me to try again, especially in view of the wide interest in the nature of the iron–oxygen bond5–7.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

References

  1. 1

    Kendrew, J. C. et al. Nature 185, 422–427 (1960).

  2. 2

    Takano, T. J. molec. Biol. 110, 569–584 (1977).

  3. 3

    Norvell, J. C., Nunes, A. C. & Schoenborn, B. P. Science 190, 568–570 (1975).

  4. 4

    Watson, H. C. & Nobbs, C. L. Colloquium Ges. biol. Chem. 19, 37–48 (Springer, Berlin, 1968).

  5. 5

    Pauling, L. Nature 203, 182–183 (1964).

  6. 6

    Weiss, J. J. Nature 202, 83–84 (1964).

  7. 7

    Griffith J. S. Proc. R. Soc. A 235, 23–26 (1956).

  8. 8

    Takano, T. J. molec. Biol. 110, 537–568 (1977).

  9. 9

    Collman, J. P., Gagne, R. R., Reed, C. A., Robinson, W. T. & Rodley, G. A. Proc. natn. Acad. Sci. U.S.A. 71, 1326–1329 (1974).

  10. 10

    Jameson, G. B. et al. Inorg. Chem. (in the press).

  11. 11

    Fermi, G. J. molec. Biol. 97, 237–256 (1975).

  12. 12

    Ladner, R. C., Heidner, E. J. & Perutz, M. F. J. molec. Biol. 114, 385–414 (1977).

Download references

Author information

Rights and permissions

Reprints and Permissions

About this article

Further reading

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.