Proteins are nature's premier building blocks for constructing complex biological devices or sophisticated coordination complexes with diverse metal-based functions (i.e., metalloproteins and metalloenzymes). Indeed, a considerable fraction of natural metalloenzymes are self-assembled multi-protein architectures with interfacial metal centers, including some prominent ones like photosystem II, nitrogenase, and cytochrome c oxidase. Yet, as chemists, our ability to control the self-assembly of proteins or to use them as synthetic building blocks for inorganic coordination chemistry has been limited. To address this shortcoming, my group has endeavored to establish design principles and experimental strategies for the metal-directed self-assembly of proteins and their utilization as platforms for coordination chemistry. In this context, we have constructed a series of metal-templated supramolecular protein complexes, which vary in their flexibilities/rigidities and present "evolutionarily naive" interfaces where functional metal coordination sites can be constructed. This presentation will cover some of the latest developments in this research project.

Engineering bioinorganic functions through metal-directed protein self-assembly

255th National Meeting (2018)

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