Abstract
THE electron spin resonance method is capable of giving fairly detailed information concerning the electron structure of molecules having unpaired electrons. In the past few years D. J. E. Ingram et al. have made detailed investigations of the electron spin resonance absorption of single crystals of hæmoglobin and myoglobin compounds. The most accurate measurements on high-spin ferri-hæmoglobin and ferrimyoglobin compounds have been made at liquid air or liquid hydrogen temperatures and a well-defined variation of g-value from g = 2 to g = 6 was obtained1–4. Very similar g-values were observed in polycrystalline samples of the prosthetic group hæmin at liquid air temperatures1,2,5. No electron spin resonance spectrum was obtained in hæmatin. Measurements in frozen aqueous solutions at 170° K on some hæmoproteins have been reported by A. Ehrenberg6. I have recently summarized much of this work up to the first part of 19637.
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SCHOFFA, G. Electron Spin Resonance in Hæmin, Hæmatin and Hæmoglobin at 4.2° K. Nature 203, 640–641 (1964). https://doi.org/10.1038/203640a0
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DOI: https://doi.org/10.1038/203640a0
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