Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins

Mann, Samuel and Heinisch, Tillmann and Ward, Thomas R. and Borovik, A. S.. (2017) Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins. Journal of the American Chemical Society, 139 (48). pp. 17289-17292.

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Official URL: http://edoc.unibas.ch/58965/

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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.
Faculties and Departments:05 Faculty of Science > Departement Chemie > Chemie > Bioanorganische Chemie (Ward)
UniBasel Contributors:Ward, Thomas R. R. and Heinisch, Tillmann
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Chemical Society
Note:Publication type according to Uni Basel Research Database: Journal article
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edoc DOI:
Last Modified:23 Jun 2020 13:28
Deposited On:22 Jan 2018 13:03

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