A Mixed‐Valent, Unsymmetrical FeIIFeIII Complex with a Terminal Phenolato Ligand as a Model for the Active Site of Purple Acid Phosphatases

Abstract

The structure and the magnetic and electrochemical properties of the active center of purple acid phosphatases are modeled by a complex that mimics the terminal coordination of the tyrosine residue and was prepared with a new heptadentate phenola‐to ligand system. The instability of the reduced FeIIFeII state of the enzyme may be attributed to the terminal ligand, since the phenolato ligand in the model is a destabilizing factor.