Designing organic frameworks for metal complexes that control the structure and function of metal centers is a synthetic challenge. Metalloproteins are examples of natural systems that achieve a high degree of functional control by regulating the microenviroments around metal centers. These proteins provide a multitude of covalent and noncovalent interactions, such as hydrogen bonding, to isolate the metal-binding sites and allow reactivity to occur. We use a bioinspired approach to design small organic ligands that bind and isolate metal ions while providing for intramolecular hydrogen bonds. The work described herein presents an alternative approach: the engineering of an artificial metalloprotein to serve as a scaffold for a copper system by employing the biotin-Streptavidin technology. The protein can be modified chemogenetically to provide point mutations to amino acid residues that modify the microenvironment of the Cu(II) ions, and the complexes can be altered chemically to tune the inter�copper ion distance across the protein dimer interface. These complexes are studied both spectroscopically as well as structurally with X�ray crystallography.

Streptavidin as a host for copper complexes

248th National Meeting (2014)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.