Abstract
SEVERAL molecules containing a porphin ring, of similar central structures, possess intermediate states when undergoing oxidation, and there has been considerable speculation on the actual nature of these transient compounds1,2. Most interest has probably been centred on the oxidation of hæmoglobin derivatives, and the action of hydrogen peroxide, potassium periodate and other oxidizing agents has been studied in detail by George and Irvine2. The two possible structures for the oxidation state of the met-hæmoglobins are: (1) a radical species formed by hydrogen atom removal from some position in the conjugated ring system, or (2) a change in the valency of the central iron atom. Although several different chemical reactions were studied it was not possible to prove conclusively which of the two structures was actually present.
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References
Cahill, A. E., and Taube, H., J. Amer. Chem. Soc., 73, 2847 (1951).
George, P., and Irvine, D. H., Biochem. J., 52, 511 (1952); 58, 188 (1954); 60, 596 (1955).
George, P., Ingram, D. J. E., and Bennett, J. E., J. Amer. Chem. Soc. (in the press).
Ingram, D. J. E., “Spectrocopy at Radio and Microwave Frequencies”, 66 (Butterworths, Ltd., 1955).
Ingram, D. J. E., Bennett, J. E., George, P., and Goldstein, J. M., J. Amer. Chem. Soc., 78, 3545 (1956).
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GIBSON, J., INGRAM, D. Location of Free Electrons in Porphin Ring Complexes. Nature 178, 871–872 (1956). https://doi.org/10.1038/178871b0
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DOI: https://doi.org/10.1038/178871b0
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