PNNL

Abstract

Catalysis enables many attributes of modern life ranging from fuels, products and energy storage and conversion, and advances in catalysis in recent years have continued to allow us to realize higher efficiencies and new processes. Combining high turnover rates and high selectivity with conversions at lower temperatures and pressures, preferably using non-precious metals as catalysts would enable the decentralized operation to produce chemicals or create energy carriers on demand at locations where we are able to harvest or store wind and solar power. The remarkable turnover frequency and selectivity of enzymes demonstrate that nature has realized these boundary conditions. We currently think that the complexity of the enzyme structure, specifically the protein scaffold, is critical to achieve this performance. Recreating this environment has been a much strived for target for decades and while the progress is impressive, we are still more in a phase of understanding than of creating de novo active catalysts that would rival enzymes performance, while also sustaining turnover. In this perspective we will identify and compare four areas where progress in functionally synthetically creating features of the enzyme scaffold: (i) confinement to enhance catalytic activity; (i) proton transport; (iii) tailoring the environment around the active site; (iv) cooperativity. For each area we outline the current state and indicate the most fruitful paths to future progress.