ArticleNature chemical biology2024
Architecture of the RNF1 complex that drives biological nitrogen fixation.
Article in Nature chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Enhancing biological nitrogen fixation in rice paddy ecosystems: challenges, opportunities, and sustainable strategies.Frontiers in microbiology · 2026Review
- The RNF/NQR redox pumps: a versatile system for energy transduction in bacteria and archaea.Applied microbiology and biotechnology · 2025Review
- Flavin transferase ApbE: From discovery to applications.The Journal of biological chemistry · 2025Review
- Molecular principles of redox-coupled sodium pumping of the ancient Rnf machinery.Nature communications · 2025Article
- Article
- Protein interactions in human pathogens revealed through deep learning.Nature microbiology · 2024Article
- A new twist to increase ion flow.Nature chemical biology · 2024Article
- Chains of death.Nature chemical biology · 2024Article
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Authors and funding
2 authors.
Funding
Abstract
Biological nitrogen fixation requires substantial metabolic energy in form of ATP as well as low-potential electrons that must derive from central metabolism. During aerobic growth, the free-living soil diazotroph Azotobacter vinelandii transfers electrons from the key metabolite NADH to the low-potential ferredoxin FdxA that serves as a direct electron donor to the dinitrogenase reductases. This process is mediated by the RNF complex that exploits the proton motive force over the cytoplasmic membrane to lower the midpoint potential of the transferred electron. Here we report the cryogenic electron microscopy structure of the nitrogenase-associated RNF complex of A. vinelandii, a seven-subunit membrane protein assembly that contains four flavin cofactors and six iron-sulfur centers. Its function requires the strict coupling of electron and proton transfer but also involves major conformational changes within the assembly that can be traced with a combination of electron microscopy and modeling.
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