Nature employs metalloproteins to mediate chemical transformations with rates and selectivities not yet achieved in synthetic systems. The efficiency of metalloproteins has been attributed in part to the control of the local environments surrounding their functional active metal center(s). This control is often achieved by non-covalent interactions including hydrogen bonds (H-bonds). In synthetic systems, it has been difficult to establish similar intramolecular hydrogen bonding (H-bonding) networks. To overcome these structural challenges, we are designing artificial metalloproteins in which the local environments around synthetic metal complexes can be modulated with a protein host. Biotin-streptavidin (Sav) technology is used as the basis to develop our artificial metalloproteins. The high binding affinity of Sav for biotin (K<sub>d</sub> ~ 10<sup>-15</sup> M) provides reproducible placement of artificial biotinylated metallocofactors within the protein host. Additionally, site-directed mutagenesis is used to install varied amino acid residues within the active site" that function as either ligands to the immobilized metal center or to modulate local environments. Using this approach, biotinylated metal complexes have been synthesized and inserted into several variants of Sav to study the effects of varying the local environment around the metal center. This presentation will show results of our newest artificial Fe proteins in which the structures of immobilized metal sites determined from X-ray diffraction methods are compared to spectroscopic and reactivity studies done in solution.

Artificial iron proteins using biotin-streptavidin technology

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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