Download MendeleyPeroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins.
Mann, S.I., Heinisch, T., Ward, T.R., Borovik, A.S.(2017) J Am Chem Soc 139: 17289-17292
- PubMed: 29117678
- DOI: https://doi.org/10.1021/jacs.7b10452
- Primary Citation of Related Structures:
5WBA, 5WBB, 5WBD, 6ANX - PubMed 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.
Organizational Affiliation:
Department of Chemistry, University of California , 1102 Natural Science II, Irvine, California 92697, United States.
