The efficient production of carbon-neutral fuels is one of the primary challenges faced by the catalysis field. Understanding how to selectively reduce CO<sub>2</sub> and utilize CO for the generation of targeted products remains an area of active research. Nature has solved this problem through the use of highly efficient chemical cascades, which decouple the reactions of CO<sub>2</sub> reduction from carbon-carbon bond formation in large, multicomponent metalloenzymes. These systems integrate local electronic control with secondary sphere effects, long-range electron transfer, substrate channeling, and dynamic conformational changes, accessing an array of complexity that remains out of reach in synthetic systems. We have approached this challenge through the use of model metalloprotein scaffolds, which are robust towards modification and provide a well-defined secondary sphere and outer coordination environment. In this talk, I will present recent work demonstrating the installation of a site-differentiated [Ni-Fe-S] cluster into a canonical ferredoxin (NiFeFd) to generate a model of the [Ni-Fe-S] cluster in native carbon monoxide dehydrogenase (CODH). This system serves as both a structural and electronic mimic of the native enzyme. The reactivity of NiFeFd towards redox transformations and interactions with native CODH substrates and inhibitors will be presented, along with the electronic structure contributions mediating these processes. Approaches for the rational design of NiFeFd using protein engineering strategies and resultant outcomes will be discussed.

Reconstructing nature’s energy conversion pathways one carbon at a time: Modeling carbon monoxide dehydrogenase in robust metalloprotein scaffolds

ACS Fall 2021

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