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. © 2012 The Royal Society of Chemistry.