Production of a ‘Cytochrome c’ with Myoglobin-like Properties by Alkylating the Cyanide Complex with Bromoacetate


THAT the iron atom of cytochrome c is bound by the imidazole rings of two histidine residues was first suggested by Theorell and Akesson1. An investigation of the effect of pH on the equilibria between ferricytochrome c and ionic ligands such as CN and N3 provided physicochemical evidence for the presence of at least one Fe-histidine bond in the oxidized state of the molecule2. If this bond is broken, as for example when a complex of ferricytochrome c with a ligand is formed, the imidazole nitrogen liberated from iron co-ordination should become available for reactions that do not take place with the native molecule. Further confirmation of this structure should thus be possible by more direct chemical observations.

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    Theorell, H., and Akesson, A., J. Amer. Chem. Soc., 63, 1812, 1818, 1820 (1941).

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    George, P., Glauser, S. C., and Schejter, A., in Molecular Basis for Enzyme Action and Inhibition, edit. by Desnuelle, P., Proc. Fifth Cong. Biochem., Moscow, 1961, 4, 192 (Pergamon Press, Oxford, 1963).

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    George, P., and Lyster, R. L. J., Proc. U.S. Nat. Acad. Sci., 44, 1013 (1958).

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    See Lemberg, R., and Legge, J. W., Hematin Compounds and Bile Pigments (Interscience, New York, 1949).

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    Scheller, W., Salewski, A., and Jung, F., Biochem. Z., 326, 288 (1955).

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    George, P., Lyster, R. L. J., and Beetlestone, J., Nature, 181, 1534 (1958).

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SCHEJTER, A., GEORGE, P. Production of a ‘Cytochrome c’ with Myoglobin-like Properties by Alkylating the Cyanide Complex with Bromoacetate. Nature 206, 1150–1151 (1965) doi:10.1038/2061150a0

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