ReviewCurrent opinion in chemical biology2016
Maturation of nitrogenase cofactor-the role of a class E radical SAM methyltransferase NifB.
Review in Current opinion in chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 37 citations in OpenAlex.
- Trafficking of a nitrogenase FeMo-cofactor assembly intermediate.Nature chemical biology · 2026Article
- Structure and Catalytic Mechanism of Radical SAM Methylases.Life (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
- Functional Diversity of HemN-like Proteins.ACS bio & med chem Au · 2022Review
- Identification of Nitrogen Fixation Genes inMicroorganisms · 2020Article
- Reactivity, Mechanism, and Assembly of the Alternative Nitrogenases.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
- Probing the coordination and function of FeNature communications · 2018Article
- Enhanced Solubilization of Class B Radical S-Adenosylmethionine Methylases by Improved Cobalamin Uptake in Escherichia coli.Biochemistry · 2018Article
- TsrM as a Model for Purifying and Characterizing Cobalamin-Dependent Radical S-Adenosylmethionine Methylases.Methods in enzymology · 2017Article
- On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes.Frontiers in chemistry · 2017Review
- Catalytic Promiscuity of the Radical S-adenosyl-L-methionine Enzyme NosL.Frontiers in chemistry · 2016Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Nitrogenase catalyzes the important reactions of N2-reduction, CO-reduction and CO2-reduction at its active cofactor site. Designated the M-cluster, this complex metallocofactor is assembled through the generation of a characteristic 8Fe-core before the insertion of Mo and homocitrate that completes the stoichiometry of the M-cluster. NifB catalyzes the crucial step of radical SAM-dependent carbide insertion that occurs concomitant with the insertion a '9th' sulfur and the rearrangement/coupling of two 4Fe-clusters into a complete 8Fe-core of the M-cluster. Further categorization of a family of NifB proteins as a new class of radical SAM methyltransferases suggests a general function of these proteins in complex metallocofactor assembly and provides a new platform for unveiling unprecedented chemical reactions catalyzed by biological systems.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.