5WBA

Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins.

(2017) J Am Chem Soc 139: 17289-17292

• PubMed: 29117678 Search on PubMedSearch on PubMed Central
• 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.

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Organizational Affiliation: 

Department of Chemistry, University of California , 1102 Natural Science II, Irvine, California 92697, United States.