About This Project

Unlike traditional chemical industry, enzymatic syntheses align with green chemistry principles, affording unmatched selectivity and fostering eco-friendly chemical conversions. In this proposal, we aim to engineer a hemoprotein for facile construction of pivotal C–N bonds. This innovative enzymatic platform seeks to convert feedstock chemicals into value-added compounds, such as aminoketones, ushering synthetic chemistry into a sustainable, efficient, and environmentally conscious age.

Ask the Scientists

What is the context of this research?

The chemical industry has a huge impact on society: this sector produces a vast array of products in every aspect of our daily lives. These myriad contributions come with considerable downsides, including the heavy environmental footprint of its production processes, which generate substantial amounts of greenhouse gases and toxic chemical wastes. One path toward more sustainable chemical synthesis is the increased utilization of enzymes. Enzymes exhibit extraordinary abilities in constructing molecules with high activity, selectivity, and sustainability—using biocatalysis in chemical production can greatly reduce toxic waste and the carbon footprint of the chemical industry. We are expanding the repertoire of biocatalysis with reactions that are useful.

What is the significance of this project?

Traditional synthesis of some bioactive molecules, which constitute a multi-billion-dollar market in the pharmaceutical industry, often requires energy-intensive, multi-step chemical processes that generate significant waste, like noble metals and organic solvents. Developing an enzymatic approach to construct those molecules not only aligns with the tenets of green chemistry but also delivers unparalleled selectivity, a cornerstone for efficient drug development. We aim to engineer a hemoprotein to facilitate the precise and efficient incorporation of functional groups into diverse molecular structures. This new-to-nature enzymatic platform will leverage the ability of enzymes to transform simple feedstock chemicals into valuable pharmaceutical compounds bearing an array of motifs.

What are the goals of the project?

The primary objective is to engineer a thermostable hemoprotein that facilitates the enzymatic construction of bioactive molecules through an efficient biocatalytic transformation. Leveraging the power of directed evolution, we intend to introduce and select for mutations that enhance the desired activity, which is present as a ‘promiscuous’ activity of various hemoproteins. Building on this, we can extend this methodology to synthesize other molecular moieties by tuning the substrate structures. The second objective is to show gram-scale enzymatic synthesis which is critical for industrial application. Ultimately, our vision is to establish an efficient and eco-friendly enzymatic platform capable of forging valuable molecules from low-cost feedstock chemicals.