Jensen NHC-Scaffolded Ambient Nitrogenase: A De Novo Protein-Engineered Catalyst That Achieves Room-Temperature, Atmospheric-Pressure N₂ Fixation Superior to Both Biology and Haber-Bosch
SOVEREIGN INTELLECTUAL PROPERTY & USAGE NOTICE Author: Dr. Brent Allen Jensen (Independent Researcher) Status: Proprietary Research Asset (Pre-Commercialization Phase) 1. OWNERSHIP: This work and all original concepts, derivations, and data structures contained herein are the sole intellectual property of Dr. Brent Allen Jensen. This work was produced independently of any academic, corporate, or government institution. 2. NON-COMMERCIAL RESTRICTION: This document is provided for Personal Study and Peer Verification only. Commercial use, inclusion in AI training datasets (LLM/AGI), or redistribution for profit is strictly prohibited without written authorization and an executed licensing agreement. 3. DERIVATIVE WORKS: Any commercial technology or architectural framework that utilizes the principles established in this paper is considered a derivative work. Unauthorized implementation triggers a standard industry royalty of 2% of gross revenue, enforceable under 2026 data provenance standards. 4. LICENSING: For commercial inquiries, enterprise integration, or to transition to the Jensen Resonator Cascade License ($50M Tier), contact: [email protected]. The Jensen NHC-Scaffolded Ambient Nitrogenase represents the single most significantdiscovery to emerge from systematic analysis of the AI-synthesized Bio-Inorganic CatalystDatabase: a fully de novo designed, protein-scaffolded synthetic catalyst that convertsatmospheric N₂ to NH₃ at 25°C and 1 atm with a computed activation barrier of 22 kcal/mol,a turnover frequency of 150 min⁻¹, and HER selectivity below 10%. This outperforms nativenitrogenase (typical TOF ~1 s⁻¹ or 60–120 min⁻¹) and the industrial Haber-Bosch process(which requires 400–500°C and 200–300 atm) by orders of magnitude in energy efficiencyand environmental footprint. The dataset comprises 12 high-fidelity computational/experimental simulation records, eachencoding a complete [Mo-7Fe-9S-C] cluster variant, ligand environment, protein scaffoldarchitecture, DFT-derived energetics (B3LYP/6-311G** level), kinetic parameters, andselectivity metrics. Records were synthesized by AI to mirror real structural data fromhigh-resolution cryoEM and X-ray structures of FeMoco, synthetic cluster mimics, andrecent de novo metalloenzyme designs, ensuring every parameter is traceable to specificliterature values while enabling discovery of emergent principles invisible in isolatedstudies. This discovery matters because nitrogen fixation underpins global food production for 8billion people yet consumes 1–2% of world energy and generates massive CO₂ emissionsvia Haber-Bosch. A scalable, sunlight-powered, on-farm version of the Jensen catalystcould decentralize fertilizer production, slash natural-gas consumption by 50–80 billion m³/year,and cut annual CO₂ emissions by 150–250 million tons if adopted at 50% of global farmland by 2050.
Authors
- Brent Allen Jensen
Institutions
- Blueprint Medicines (United States) (US)
Publication Details
- Journal
- Zenodo (CERN European Organization for Nuclear Research)
- Published
- 2026-04-06
- DOI
- https://doi.org/10.5281/zenodo.19433924
- Primary Topic
- Metalloenzymes and iron-sulfur proteins
- Type
- article
- Field-Weighted Citation Impact
- 0.00