Modification of Heme Peptides by Reverse Proteolysis: Spectroscopy of Microperoxidase-10 with C-Terminal Histidine, Tyrosine, and Methionine Residues

摘要

In accord with observation, our results suggest that histidine ligation will be favored in misfolded forms of cyt c. Although a tyrosine hydroxyl may be able to coordinate at high pH, it is unlikely that a methionine thioether will bind to Fe- (Ⅲ) in any undolded state of the protein.