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. 1974 Jul;71(7):2892–2894. doi: 10.1073/pnas.71.7.2892

Alkaline Isomerization of Ferricytochrome c: Identification of the Lysine Ligand

Harvey Wilgus 1, Earle Stellwagen 1
PMCID: PMC388578  PMID: 4368392

Abstract

Changes in the visible absorbance spectra of complexes of horse heart cytochrome c hemopeptide 1-65, peptide 66-104, and their guanidinated counterparts are compared with those characteristic of native and fully guanidinated ferricytochrome c over the pH range 7 to 11. Upon raising the pH, the methionine ligand in the guanidinated hemopeptide 1-65·peptide 66-104 complex is replaced by a strong field ligand. By contrast, the methionine ligand in the hemopeptide 1-65·guanidinated peptide 66-104 is replaced by a weak field ligand. These results demonstrate that lysine 13 does not ligate with the heme iron upon isomerization of ferricytochrome c and that the ligand in the horse heart protein is one of the eight lysine residues in the 66-104 segment of the polypeptide, most likely lysine 79.

Keywords: heme protein, peptide reconstitution, guanidination

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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