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Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins.


ABSTRACT: 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.

SUBMITTER: Mann SI 

PROVIDER: S-EPMC5747327 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

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Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins.

Mann Samuel I SI   Heinisch Tillmann T   Ward Thomas R TR   Borovik A S AS  

Journal of the American Chemical Society 20171115 48


Copper-hydroperoxido species (Cu<sup>II</sup>-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<sup>II</sup>-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 hydrog  ...[more]

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