Issue 35, 2018

Coordination chemistry within a protein host: regulation of the secondary coordination sphere

Abstract

Secondary coordination spheres of metal complexes are instrumental in controlling properties that are linked to function. To study these effects in aqueous solutions artificial Cu proteins have been developed using biotin–streptavidin (Sav) technology and their binding of external azide ions investigated. Parallel binding studies were done in crystallo on single crystals of the artificial Cu proteins. Spectroscopic changes in solution are consistent with azide binding to the Cu centers. Structural studies corroborate that a Cu–N3 unit is present in each Sav subunit and reveal the composition of hydrogen bonding (H-bonding) networks that include the coordinated azido ligand. The networks involve amino acid residues and water molecules within the secondary coordination sphere. Mutation of these residues to ones that cannot form H-bonds caused a measurble change in the equilibrium binding constants that were measured in solution. These findings further demonstrate the utility of biotin–Sav technology to prepare water-stable inorganic complexes whose structures can be controlled within both primary and secondary coordination spheres.

Graphical abstract: Coordination chemistry within a protein host: regulation of the secondary coordination sphere

Supplementary files

Article information

Article type
Communication
Submitted
10 Mar 2018
Accepted
03 Apr 2018
First published
03 Apr 2018

Chem. Commun., 2018,54, 4413-4416

Coordination chemistry within a protein host: regulation of the secondary coordination sphere

S. I. Mann, T. Heinisch, T. R. Ward and A. S. Borovik, Chem. Commun., 2018, 54, 4413 DOI: 10.1039/C8CC01931B

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