ArticleFrontiers in plant science2017
Diversity and Functional Analysis of the FeMo-Cofactor Maturase NifB.
Article in Frontiers in plant science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- A high-throughput heterologous expression platform for plant synthetic biology based on Arabidopsis suspension cells.Journal of experimental botany · 2026Article
- Computationally Guided Design of a Soluble, Abundant and Functional AnfH Variant for the Expression of Fe-Only Nitrogenase in Plant Mitochondria.Plant biotechnology journal · 2025Article
- Article
- Structure and Catalytic Mechanism of Radical SAM Methylases.Life (Basel, Switzerland) · 2022Review
- Nitrogenase Cofactor Maturase NifB Isolated from Transgenic Rice is Active in FeMo-co Synthesis.ACS synthetic biology · 2022Article
- Article
- Functional analysis of multiple nifB genes of Paenibacillus strains in synthesis of Mo-, Fe- and V-nitrogenases.Microbial cell factories · 2021Article
- Exploiting genetic diversity and gene synthesis to identify superior nitrogenase NifH protein variants to engineer NCommunications biology · 2021Article
- A CRISPRi-dCas9 System for Archaea and Its Use To Examine Gene Function during Nitrogen Fixation by Methanosarcina acetivorans.Applied and environmental microbiology · 2020Article
- Biosynthesis of Nitrogenase Cofactors.Chemical reviews · 2020Review
- Biosynthesis of the nitrogenase active-site cofactor precursor NifB-co inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- State of the art in eukaryotic nitrogenase engineering.FEMS microbiology letters · 2018Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
One of the main hurdles to engineer nitrogenase in a non-diazotrophic host is achieving NifB activity. NifB is an extremely unstable and oxygen sensitive protein that catalyzes a low-potential SAM-radical dependent reaction. The product of NifB activity is called NifB-co, a complex [8Fe-9S-C] cluster that serves as obligate intermediate in the biosyntheses of the active-site cofactors of all known nitrogenases. Here we study the diversity and phylogeny of naturally occurring NifB proteins, their protein architecture and the functions of the distinct NifB domains in order to understand what defines a catalytically active NifB. Focus is on NifB from the thermophile
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