Redox tuning of two biological copper centers through non-covalent interactions: same trend but different magnitude

Abstract

The same non-covalent interactions previously found to affect the redox potential (E_m) of the mononuclear T1 Cu protein azurin (Az) are shown to also fine-tune the E_m of the dinuclear Cu_A center in the same Az protein scaffold. The effects of these mutations are in the same direction but with smaller magnitude in the Cu_A site, due to dissipation of the effects by the dinuclear Cu_A center.