Letter | Published:

Thermodynamic Data for Myoglobin, Hæmoglobin and Cytochrome-c Reactions, and the Position of the Hæm Groups

Naturevolume 175page1034 (1955) | Download Citation

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Abstract

CONANT1 first put forward the idea that the hæms in hæmoglobin are held by two bonds of unequal strength between the iron and groups in the protein on both sides of the hæm disk, the weaker bond breaking when combination with oxygen, carbon monoxide, etc., occurs. This crevice configuration has been elaborated to explain various features of its reactions by Coryell and Pauling, Wyman, and St. George and Pauling; but Keilin has laid stress on other aspects, particularly the combination with large molecules such as nitrosobenzene and 4-methyl imidazole, which suggest that the hæm iron is not embedded in a crevice but is readily accessible2.

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References

  1. 1

    Conant, J. B., Harvey Lectures, 28, 159 (1932–33).

  2. 2

    Keilin, D., Nature, 171, 922 (1953), with ref. to Coryell and Pauling, etc.

  3. 3

    Kendrew, J. C., and Parrish, R. G., Nature, 175, 206 (1955).

  4. 4

    see Margoliash, E., Nature, 175, 293 (1955).

  5. 5

    George, P., and Tsou, C. L., Biochem. J., 50, 440 (1952).

  6. 6

    George, P., and Hanania, G. I. H. (unpublished results).

  7. 7

    George, P., and Hanania, G. I. H., Biochem. J., 52, 517 (1952); 55, 236 (1953).

  8. 8

    Scheler, W., and Jung, F., Biochem. Z., 325, 515 (1954).

  9. 9

    George, P., “Currents in Biochemical Research”, 2 (Interscience, New York, in the press).

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Author information

Affiliations

  1. Department of Colloid Science, University, Cambridge

    • PHILIP GEORGE
    •  & G. I. H. HANANIA

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https://doi.org/10.1038/1751034a0

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