Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins

Abstract

Copper–hydroperoxido species (Cu II –OOH) have been proposed to be key intermediates in biological and synthetic oxidations. Using biotin–streptavidin (Sav) technology, artificial copper proteins have been developed to stabilize a Cu II –OOH complex in solution and in crystallo . Stability is achieved because the Sav host provides a local environment around the Cu–OOH that includes a network of hydrogen bonds to the hydroperoxido ligand. Systematic deletions of individual hydrogen bonds to the Cu–OOH complex were accomplished using different Sav variants and demonstrated that stability is achieved with a single hydrogen bond to the proximal O-atom of the hydroperoxido ligand: changing this interaction to only include the distal O-atom produced a reactive variant that oxidized an external substrate