Nitrogen is ubiquitous in biomolecules, natural products, and synthetic compounds, all tracing back to atmospheric N₂. However, breaking the strong N₂ bond under ambient conditions remains a major challenge. The Haber-Bosch process, though effective, consumes ~2% of global energy and emits ~1.2% of CO₂ annually. In contrast, nitrogenases perform this reaction under mild conditions, but practical translation has proven elusive.

We report the computational design of the first artificial nitrogenase that binds the native iron-molybdenum cofactor (FeMoco) and reduces N₂ to NH₃. Acetylene reduction assays and EPR confirmed FeMoco binding. Excitingly, ¹⁵N₂ reduction to ¹⁵NH₄⁺ was observed via ¹H-NMR using quantum dots.

This small, stable, monomeric protein, free of additional cofactors or subunits, provides a simplified system for studying N₂ fixation and advancing next-generation catalysts. It also marks a major milestone in metalloprotein design, demonstrating successful binding of a complex metallocofactor and catalytic activity in a highly challenging reaction.

Yi Lu

The University of Texas at Austin

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