Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins

Copper–hydroperoxido species (CuII–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 CuII–OOH complex in solution and in crystallo. Stability is achieved be...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2017-12, Vol.139 (48), p.17289-17292
Main Authors: Mann, Samuel I, Heinisch, Tillmann, Ward, Thomas R, Borovik, A. S
Format: Article
Language:English
Subjects:
Copper - chemistry
Hydrogen Bonding
Ligands
Metalloproteins - chemistry
Peroxides - chemistry
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Summary:Copper–hydroperoxido species (CuII–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 CuII–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.
ISSN:0002-7863
1520-5126
DOI:10.1021/jacs.7b10452