Abstract
IN a previous communication1, it was reported that a free radical is formed during the action of hydrogen peroxide on methæmoglobin. As its g-value approximated to that of a free electron, this result was interpreted in terms of electron removal from the π-orbitals of the porphyrin ring, by analogy with the reactions occurring during the oxidation of porphyrins and phthalocyanines2. This explanation, involving the postulate of little interaction between unpaired electron and central iron atom, conflicted with the results of titration studies3, and the evidence from paramagnetic susceptibility4.
Similar content being viewed by others
References
Gibson, J. F., and Ingram, D. J. E., Nature, 178, 871 (1956).
George, P., Ingram, D. J. E., and Bennett, J., J. Amer. Chem. Soc., 79, 1870 (1957).
George, P., and Irvine, D., Biochem. J., 60, 596 (1955).
Theorell, H., and Ehrenberg, A., Arch. Biochem. Biophys., 41, 442 (1952).
George, P., and Irvine, D., Biochem. J., 52, 511 (1952).
Chance, B., and Fergusson, R. R., “The Mechanism of Enzyme Action” (The Johns Hopkins Press, Baltimore, 1954).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
GIBSON, J., INGRAM, D. & NICHOLLS, P. Free Radical produced in the Reaction of Metmyoglobin with Hydrogen Peroxide. Nature 181, 1398–1399 (1958). https://doi.org/10.1038/1811398a0
Issue Date:
DOI: https://doi.org/10.1038/1811398a0
- Springer Nature Limited
This article is cited by
-
Endonuclease-like activity of heme proteins
JBIC Journal of Biological Inorganic Chemistry (2005)
-
Lipid peroxidation and oxidation of several compounds by H2O2 activated metmyoglobin
Lipids (1985)
-
Ferrous complexes in the catalase reaction
Experientia (1963)