Abstract
CYTOCHROME c is the only well-characterized natural hæm–protein compound which, in the presence of excess acid acetone, is not split into hæmatin and protein. The stability of the hæm – protein link in cytochrome c was further emphasized when Hill and Keilin1 attempted to prepare the unmodified porphyrin of the component. In the presence of reducing agents in acid solution iron is removed, leaving an ether-insoluble porphyrin which has been shown2,3 still to contain peptide groups. From a study of this ‘porphyrin c’, Theorell4 concluded that in native cytochrome c the hæm is bound to the protein not only by linkage to the iron, but also by stable thio-ether linkages connecting the α-carbon atoms of side-chains 2 and 4 of protoporphyrin with two terminal 1-cysteine residues of the protein.
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DAVENPORT, H. Reductive Cleavage of Cytochrome c. Nature 169, 75 (1952). https://doi.org/10.1038/169075a0
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DOI: https://doi.org/10.1038/169075a0
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