Ammonia synthesis is foundational to global agriculture and chemical manufacturing, providing the primary source of fixed nitrogen for fertilizers, polymers, and pharmaceuticals. Traditional ammonia production through the Haber-Bosch process, however, operates under extreme conditions—temperatures exceeding 400°C and pressures over 150 bars—requiring massive energy inputs and fossil fuel-derived hydrogen. This results in significant carbon emissions, accounting for nearly 2% of global CO₂ output, and creates centralized infrastructures that limit access in remote or resource-limited regions. As global demand for sustainable food production and carbon neutrality increases, there is an urgent need for alternative ammonia production methods that function under mild, decentralized conditions.
Current alternatives to Haber-Bosch—including electrochemical reduction and biological nitrogen fixation—face formidable technical challenges. Electrochemical approaches suffer from low faradaic efficiencies and require rare catalysts, while biological nitrogenases are oxygen-sensitive, slow, and dependent on complex, difficult-to-stabilize cofactors. Heterogeneous catalysis typically still demands elevated temperatures or specialized equipment, preventing truly accessible, scalable solutions.
This technology introduces Artificial Nitrogenase (ArtN₂ase) enzymes—computationally engineered proteins capable of catalyzing the six-electron reduction of dinitrogen (N₂) to ammonia (NH₃) under ambient temperature and pressure conditions. Built on either native protein scaffolds or de novo AI-designed structures, these enzymes integrate either the natural FeMoco cofactor or synthetic iron-sulfur clusters into custom-tailored metal-binding pockets, with optimized electron-transfer pathways that replicate the catalytic cycle of natural nitrogenase.
ArtN₂ase bypasses the need for hydrogen gas, high temperatures, or high pressures and eliminates dependence on substrate surrogates or harsh reaction conditions. The modular design supports swapping of cofactors and repurposing the platform for nitrogen transfer or hydrogenation reactions beyond ammonia synthesis. Initial in vitro demonstrations have shown catalytic activity, with ongoing work focused on improving turnover frequency, cofactor stability, and broadening functional capabilities.