Abstract
THE investigation of single crystals of hæmoglobin derivatives by paramagnetic resonance can give two distinct types of information. First, the actual resonance conditions and the resultant g values associated with the electronic transitions will yield details on the orbitals involved in the chemical binding of the central iron atom. Secondly, the angular variation of the g values enables an accurate determination to be made of the orientation of the hæm and porphyrin planes with respect to the external crystalline axes. Although the structure of the rest of the molecule cannot be analysed directly in this way, detailed information on the orientation of the hæm planes can be combined with X-ray measurements1 to calculate the polypeptide chain directions and similar factors. It would appear that the determination of the hæm plane orientations by paramagnetic resonance is much more accurate than that by any other method so far applied.
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References
Kendrew, J. C., Acta Cryst., 1, 336 (1948).
Ingram, D. J. E., “Spectroscopy at Radio and Microwave Frequencies”, 66 (Butterworths, Ltd., 1955).
Griffith, J. S., and Stevens, K. W. H., as quoted in George, P., Bennett, J. E., and Ingram, D. J. E., J. Chem. Phys. (in the press).
Kendrew, J. C., Parrish, R. G., Marrack, J. R., and Orleans, E. S., Nature, 174, 946 (1954).
Bleaney, B., and Ingram, D. J. E., Proc. Phys. Soc., A, 65, 953 (1952).
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BENNETT, J., INGRAM, D. Analysis of Crystalline Hæmoglobin Derivatives by Paramagnetic Resonance. Nature 177, 275–276 (1956). https://doi.org/10.1038/177275a0
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DOI: https://doi.org/10.1038/177275a0
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