ArticleNature communications2023
Structural consequences of turnover-induced homocitrate loss in nitrogenase.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Function, Structure, and Regulation of Nitrogen Fixation-like Metalloproteins for Nitrogen, Energy, Carbon, and Sulfur Metabolism.Chemical reviews · 2026Review
- A Surfactant Cocktail Overcomes Air-Water Interface Artifacts in Single-Particle CryoEM.bioRxiv : the preprint server for biology · 2026Article
- Nickel-NTA lipid-monolayer affinity grids allow for high-resolution structure determination by cryo-EM.Journal of structural biology · 2025Article
- Ascorbyl Radicals as Reducing Agents in Copper-Catalyzed Redox Reactions.Inorganic chemistry · 2025Article
- CryoEM-enabled visual proteomics reveals de novo structures of oligomeric protein complexes.Structure (London, England : 1993) · 2025Article
- Article
- Cryo-EM captures the coordination of asymmetric electron transfer through a di-copper site in DPOR.Nature communications · 2025Article
- Preparation of oxygen-sensitive proteins for high-resolution cryoEM structure determination using blot-free vitrification.Nature communications · 2025Article
- The nitrogenase mechanism: new roles for the dangler?Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Review
- Methylthio-alkane reductases use nitrogenase metalloclusters for carbon-sulfur bond cleavage.Nature catalysis · 2025Article
- Structural evolution of nitrogenase states under alkaline turnover.Nature communications · 2024Article
- Anaerobic cryoEM protocols for air-sensitive nitrogenase proteins.Nature protocols · 2024Review
- Molybdenum and vanadium homocitrates and their homologs - towards the local environments and protonations of FeMo/V-cofactors in nitrogenases.Coordination chemistry reviews · 2024Article
- Mutational Analysis of the Nitrogenase Carbon Monoxide Protective Protein CowN Reveals That a Conserved C-Terminal Glutamic Acid Residue Is Necessary for Its Activity.Biochemistry · 2024Article
- Structural insights into the iron nitrogenase complex.Nature structural & molecular biology · 2024Article
- Nitrogenase beyond the Resting State: A Structural Perspective.Molecules (Basel, Switzerland) · 2023Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia during the process of biological nitrogen fixation that is essential for sustaining life. The active site FeMo-cofactor contains a [7Fe:1Mo:9S:1C] metallocluster coordinated with an R-homocitrate (HCA) molecule. Here, we establish through single particle cryoEM and chemical analysis of two forms of the Azotobacter vinelandii MoFe-protein - a high pH turnover inactivated species and a ∆NifV variant that cannot synthesize HCA - that loss of HCA is coupled to α-subunit domain and FeMo-cofactor disordering, and formation of a histidine coordination site. We further find a population of the ∆NifV variant complexed to an endogenous protein identified through structural and proteomic approaches as the uncharacterized protein NafT. Recognition by endogenous NafT demonstrates the physiological relevance of the HCA-compromised form, perhaps for cofactor insertion or repair. Our results point towards a dynamic active site in which HCA plays a role in enabling nitrogenase catalysis by facilitating activation of the FeMo-cofactor from a relatively stable form to a state capable of reducing dinitrogen under ambient conditions.
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