Heterologous synthesis of a simplified nitrogenase analog in Escherichia coli

Liu YA, Lee CC, Górecki K, Stiebritz M, Duffin C, Solomon JB, Ribbe MW, Hu Y (2025)

Publication Type: Journal article

Publication year: 2025

Journal

Science Advances American Association for the Advancement of Science

Book Volume: 11

Article Number: eadw6785

Journal Issue: 18

DOI: 10.1126/sciadv.adw6785

Abstract

The heterologous synthesis of a nitrogen-fixing system in a non-diazotrophic organism is a long-sought-after goal because of the crucial importance of nitrogenase for agronomy, energy, and the environment. Here, we report the heterologous synthesis of a two-component nitrogenase analog from Azotobacter vinelandii, which consists of the reductase component (NifH) and the cofactor maturase (NifEN), in Escherichia coli. Metal, electron paramagnetic resonance, and activity analyses verify the cluster composition and functional competence of the heterologously expressed NifH and NifEN. Nuclear magnetic resonance, nanoscale secondary ion mass spectrometry, and growth experiments further illustrate the ability of the NifH/NifEN system to reduce N2 and incorporate the reduced N into the cellular mass. These results establish NifEN/NifH as a simplified nitrogenase analog that could be optimized and engineered to facilitate transgenic expression and biotechnological adaptations of this important metalloenzyme.

Involved external institutions

University of California Irvine US United States (USA) (US)

How to cite

APA:

Liu, Y.A., Lee, C.C., Górecki, K., Stiebritz, M., Duffin, C., Solomon, J.B.,... Hu, Y. (2025). Heterologous synthesis of a simplified nitrogenase analog in Escherichia coli. Science Advances, 11(18). https://doi.org/10.1126/sciadv.adw6785

MLA:

Liu, Yiling A., et al. "Heterologous synthesis of a simplified nitrogenase analog in Escherichia coli." Science Advances 11.18 (2025).

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