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Architecture of the NADH:ferredoxin oxidoreductase RNF that drives Biological Nitrogen Fixation
Open accessPreprint — published as 10.1038/s41589-024-01641-1 · Paper page
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 cryo-EM 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. One Sentence Summary: Biological nitrogen fixation requires electrons with a negative redox potential, and the diazotroph Azotobacter vinelandii can provide these through the evolutionarily ancient RNF complex that bridges the energy difference between NADH and a low-potential ferredoxin by exploiting the transmembrane proton gradient.
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Highly accurate protein structure prediction with AlphaFold
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Metadata
- Authors
- Zhang, L., & Einsle, O.
- Affiliations
- University of Freiburg (DE)
- Corresponding author
- Einsle, Oliver
- Venue
- Nature Chemical Biology
- Publisher
- openRxiv
- Published
- 2022-07-09
- Volume
- 20
- Issue
- 8
- Pages
- 1078-1085
- ISSN
- 1552-4450 (ISSN-L)
- OpenAlex
- W4399781533
- Cited by
- 25
- References
- 1
- Citations by year
- 2026: 5 · 2025: 8 · 2024: 8 · 2023: 2 · 2022: 2
- FWCI
- 1.40
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Nature Chemical Biology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (278002225, RTG 2202, 192904750, INST 35, 46710898, CRC1381, 403222702)
- Albert-Ludwigs-Universität Freiburg
- Université de Fribourg
- FP7 Ideas: European Research Council (310656)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Physical Sciences › Chemical Engineering › Catalysis › Ammonia Synthesis and Nitrogen Reduction
- Keywords
- nitrogen fixation, Azotobacter vinelandii, NADH, electron transfer, proton motive force, flavin cofactor, iron-sulfur clusters, conformational change, dinitrogenase reductase
- MeSH terms
- Bacterial Proteins, Models, Molecular, Nitrogen Fixation, Oxidoreductases, Protein Conformation, Azotobacter vinelandii, Cryoelectron Microscopy
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