| Autor: |
Wilgus, Harvey, Stellwagen, Earle |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; July 1974, Vol. 71 Issue: 7 p2892-2894, 3p |
| Abstrakt: |
Changes in the visible absorbance spectra of complexes of horse heart cytochrome chemopeptide 1-65, peptide 66-104, and their guanidinated counterparts are compared with those characteristic of native and fully guanidinated ferricytochrome cover 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 cand 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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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