ArticleProceedings of the National Academy of Sciences of the United States of America2011
NifEN-B complex of Azotobacter vinelandii is fully functional in nitrogenase FeMo cofactor assembly.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 72 citations in OpenAlex.
- Dynamics driving the precursor in NifEN scaffold during nitrogenase FeMo-cofactor assembly.Nature chemical biology · 2026Article
- NifEN: a versatile player in nitrogenase assembly, catalysis and evolution.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Review
- Structural Insights and Mechanistic Understanding of Iron-Molybdenum Cofactor Biosynthesis by NifB in Nitrogenase Assembly Process.Molecules and cells · 2023Review
- Synthesis of a FeJournal of the American Chemical Society · 2023Article
- Nitrogenase Fe Protein: A Multi-Tasking Player in Substrate Reduction and Metallocluster Assembly.Molecules (Basel, Switzerland) · 2022Review
- Highlighting the Unique Roles of RadicalJournal of bacteriology · 2022Review
- Radical SAM-dependent formation of a nitrogenase cofactor core on NifB.Journal of inorganic biochemistry · 2022Review
- Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.Chemical reviews · 2022Review
- Evidence of substrate binding and product release via belt-sulfur mobilization of the nitrogenase cofactor.Nature catalysis · 2022Article
- An EPR and VTVH MCD spectroscopic investigation of the nitrogenase assembly protein NifB.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- Bioassembly of complex iron-sulfur enzymes: hydrogenases and nitrogenases.Nature reviews. Chemistry · 2020Article
- The Spectroscopy of Nitrogenases.Chemical reviews · 2020Review
- Biosynthesis of Nitrogenase Cofactors.Chemical reviews · 2020Review
- Electron Paramagnetic Resonance and Magnetic Circular Dichroism Spectra of the Nitrogenase M Cluster Precursor Suggest Sulfur Migration upon Oxidation: A Proposal for Substrate and Inhibitor Binding.Chembiochem : a European journal of chemical biology · 2020Article
- Spectroscopic Characterization of an Eight-Iron Nitrogenase Cofactor Precursor that Lacks the "9Angewandte Chemie (International ed. in English) · 2019Review
- Polyprotein strategy for stoichiometric assembly of nitrogen fixation components for synthetic biology.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Probing the coordination and function of FeNature communications · 2018Article
- Tracing the 'ninth sulfur' of the nitrogenase cofactor via a semi-synthetic approach.Nature chemistry · 2018Article
- Role of the nifB1 and nifB2 Promoters in Cell-Type-Specific Expression of Two Mo Nitrogenases in the Cyanobacterium Anabaena variabilis ATCC 29413.Journal of bacteriology · 2017Article
- Diversity and Functional Analysis of the FeMo-Cofactor Maturase NifB.Frontiers in plant science · 2017Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Assembly of nitrogenase FeMoco is one of the key processes in bioinorganic chemistry. NifB and NifEN are two essential elements immediately adjacent to each other along the biosynthetic pathway of FeMoco. Previously, an 8Fe-precursor of FeMoco was identified on NifEN; however, the identity of the biosynthetic intermediate on NifB has remained elusive to date. Here, we present a combined biochemical and spectroscopic investigation of a His-tagged NifEN-B fusion protein of Azotobacter vinelandii. Our data from the EPR and activity analyses confirm the presence of the 8Fe-precursor in the NifEN entity of NifEN-B; whereas those from the metal, EPR, and UV/Vis experiments reveal the presence of additional [Fe(4)S(4)]-type cluster species in the NifB entity of NifEN-B. EPR-, UV/Vis- and metal-based quantitative analyses suggest that the newly identified cluster species in NifEN-B consist of both SAM-motif (CXXXCXXC)- and non-SAM-motif-bound [Fe(4)S(4)]-type clusters. Moreover, EPR and activity experiments indicate that the non-SAM-motif [Fe(4)S(4)] cluster is a NifB-bound intermediate of FeMoco assembly, which could be converted to the 8Fe-precursor in a SAM-dependent mechanism. Combined outcome of this work provides the initial insights into the biosynthetic events of FeMoco on NifB. More importantly, the full capacity of NifEN-B in FeMoco biosynthesis demonstrates the potential of this fusion protein as an excellent platform for further investigations of the role of NifB and its interaction with NifEN during the process of FeMoco assembly.
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