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

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Abstract

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 N−3 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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References

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Author notes

  1. ABEL SCHEJTER

    Present address: Department of Biochemistry, University of Tel-Aviv, Israel

Authors and Affiliations

  1. John Harrison Laboratory of Chemistry, University of Pennsylvania, Philadelphia

    ABEL SCHEJTER & PHILIP GEORGE

Authors
  1. ABEL SCHEJTER
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  2. PHILIP GEORGE
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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). https://doi.org/10.1038/2061150a0

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