Heterologous synthesis of a simplified nitrogenase analog in <i>Escherichia coli</i>.

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 redu

SUBMITTER: Liu YA 

PROVIDER: S-EPMC12047441 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature