ArticleProceedings of the National Academy of Sciences of the United States of America2007
In vitro synthesis of the iron-molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum, and homocitrate using purified proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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48 citing papers in PubMed, 105 citations in OpenAlex.
- Dynamics driving the precursor in NifEN scaffold during nitrogenase FeMo-cofactor assembly.Nature chemical biology · 2026Article
- Investigation of themBio · 2025Article
- Carmna: classification and regression models for nitrogenase activity based on a pretrained large protein language model.Briefings in bioinformatics · 2025Article
- Iron-molybdenum cofactor synthesis by a thermophilic nitrogenase devoid of the scaffold NifEN.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Holistic view of biological nitrogen fixation and phosphorus mobilization inFrontiers in microbiology · 2023Article
- Structure and Catalytic Mechanism of Radical SAM Methylases.Life (Basel, Switzerland) · 2022Review
- Functional expression of the nitrogenase Fe protein in transgenic rice.Communications biology · 2022Article
- Nitrogenase Cofactor Maturase NifB Isolated from Transgenic Rice is Active in FeMo-co Synthesis.ACS synthetic biology · 2022Article
- Article
- Radical SAM Enzymes and Metallocofactor Assembly: A Structural Point of View.ACS bio & med chem Au · 2022Review
- Nitrogen and phosphorus significantly alter growth, nitrogen fixation, anatoxin-a content, and the transcriptome of the bloom-forming cyanobacterium,Frontiers in microbiology · 2022Article
- Article
- Biosynthesis of cofactor-activatable iron-only nitrogenase in Saccharomyces cerevisiae.Microbial biotechnology · 2021Article
- An unexpected P-cluster like intermediateChemical science · 2021Article
- Exploiting genetic diversity and gene synthesis to identify superior nitrogenase NifH protein variants to engineer NCommunications biology · 2021Article
- Use of synthetic biology tools to optimize the production of active nitrogenase Fe protein in chloroplasts of tobacco leaf cells.Plant biotechnology journal · 2020Article
- Biosynthesis of Nitrogenase Cofactors.Chemical reviews · 2020Review
- Reconstructing the evolutionary history of nitrogenases: Evidence for ancestral molybdenum-cofactor utilization.Geobiology · 2020Article
- Biosynthesis of the nitrogenase active-site cofactor precursor NifB-co inProceedings of the National Academy of Sciences of the United States of America · 2019Article
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6 authors at 1 institution in 1 country.
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Abstract
Biological nitrogen fixation, the conversion of atmospheric N2 to NH3, is an essential process in the global biogeochemical cycle of nitrogen that supports life on Earth. Most of the biological nitrogen fixation is catalyzed by the molybdenum nitrogenase, which contains at its active site one of the most complex metal cofactors known to date, the iron-molybdenum cofactor (FeMo-co). FeMo-co is composed of 7Fe, 9S, Mo, R-homocitrate, and one unidentified light atom. Here we demonstrate the complete in vitro synthesis of FeMo-co from Fe(2+), S(2-), MoO4(2-), and R-homocitrate using only purified Nif proteins. This synthesis provides direct biochemical support to the current model of FeMo-co biosynthesis. A minimal in vitro system, containing NifB, NifEN, and NifH proteins, together with Fe(2+), S(2-), MoO4(2-), R-homocitrate, S-adenosyl methionine, and Mg-ATP, is sufficient for the synthesis of FeMo-co and the activation of apo-dinitrogenase under anaerobic-reducing conditions. This in vitro system also provides a biochemical approach to further study the function of accessory proteins involved in nitrogenase maturation (as shown here for NifX and NafY). The significance of these findings in the understanding of the complete FeMo-co biosynthetic pathway and in the study of other complex Fe-S cluster biosyntheses is discussed.
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