Alkaline isomerization of ferricytochrome c: identification of the lysine ligand.
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.
D000818:Animals; D003574:Cytochrome c Group / Q000378:metabolism*; D006146:Guanidines; D006418:Heme; D006736:Horses; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007501:Iron / Q000378:metabolism*; D008024:Ligands; D008239:Lysine; D008715:Methionine; D009206:Myocardium / Q000378:metabolism; D013056:Spectrophotometry, Ultraviolet
D003574:Cytochrome c Group; D006146:Guanidines; D008024:Ligands; D006418:Heme; D008715:Methionine; D007501:Iron; D008239:Lysine