Alkaline Isomerization of Ferricytochrome c: Identification of the Lysine Ligand
AUTOR(ES)
Wilgus, Harvey
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=388578Documentos Relacionados
- Electron Transfer to Ferricytochrome c: Reaction with Hydrated Electrons and Conformational Transitions Involved
- Monensin blocks the maturation of receptors for insulin and somatomedin C: Identification of receptor precursors
- "Hepatite C: transmissão entre casais"
- Hepatitis C: genotyping
- Electron Transfer Reactions in Biological Systems: The Reduction of Ferricytochrome c by Chromous Ions
