Structural highlights
Function
[SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
Publication Abstract from PubMed
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.
Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins.,Mann SI, Heinisch T, Ward TR, Borovik AS J Am Chem Soc. 2017 Nov 15. doi: 10.1021/jacs.7b10452. PMID:29117678[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mann SI, Heinisch T, Ward TR, Borovik AS. Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins. J Am Chem Soc. 2017 Nov 15. doi: 10.1021/jacs.7b10452. PMID:29117678 doi:http://dx.doi.org/10.1021/jacs.7b10452
