5WBB

Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins - S112A

Summary for 5WBB

• Entry DOI: 10.2210/pdb5wbb/pdb
• Descriptor: Streptavidin, [N-(2-{bis[2-(pyridin-2-yl-kappaN)ethyl]amino-kappaN}ethyl)-5-(2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamide]copper, COPPER (II) ION, ... (6 entities in total)
• Functional Keywords: streptavidin, biotin, copper, hydroperoxo, secondary coordination sphere, hydrogen bond, biotin binding protein, metal binding protein
• Biological source: Streptomyces avidinii
• Cellular location: Secreted: P22629
• Total number of polymer chains: 1
• Total formula weight: 17365.93

Authors

Mann, S.I.,Heinisch, T.,Ward, T.R.,Borovik, A.S. (deposition date: 2017-06-28, release date: 2017-11-22, Last modification date: 2023-10-04)

Primary citation

Mann, S.I.,Heinisch, T.,Ward, T.R.,Borovik, A.S.
Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins.
J. Am. Chem. Soc., 139:17289-17292, 2017

PubMed Abstract: Copper-hydroperoxido species (Cu-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-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.

PubMed: 29117678
DOI: 10.1021/jacs.7b10452

Experimental method

X-RAY DIFFRACTION (1.5 Å)