Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Role of Azotobacter vinelandii FdxN in FeMo-co biosynthesis.

FEBS letters - 31 Jan 2014

Jiménez-Vicente Emilio, Navarro-Rodríguez Mónica, Poza-Carrión César, Rubio Luis M

Abstract excerpt

Biosynthesis of metal clusters for the nitrogenase component proteins NifH and NifDK involves electron donation events. Yet, electron donors specific to the biosynthetic pathways of the [4Fe-4S] cluster of NifH, or the P-cluster and the FeMo-co of NifDK, have not been identified. Here we show that an Azotobacter vinelandii mutant lacking fdxN was specifically impaired in FeMo-co biosynthesis. The ΔfdxN mutant...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Nitrogenase
Share to Azotobacter vinelandii
Share to Biosynthetic Pathways

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Electrons

Share to Mutation

Share to Oxidoreductases

Source

Identifiers

PMID: 24374338
DOI: 10.1016/j.febslet.2013.12.018

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of Azotobacter vinelandii FdxN in FeMo-co biosynthesis.PMID 24374338Read ↗

A proposed role for the Azotobacter vinelandii NfuA protein as an intermediate iron-sulfur cluster carrier.Semantic proximity Read ↗

Accumulation of 55Fe-labeled precursors of the iron-molybdenum cofactor of nitrogenase on NifH and NifX of Azotobacter vinelandii.Semantic proximity Read ↗

Evidence for nifU and nifS participation in the biosynthesis of the iron-molybdenum cofactor of nitrogenase.Semantic proximity Read ↗

Nitrogenase-catalyzed ethane production and CO-sensitive hydrogen evolution from MoFe proteins having amino acid substitutions in an alpha-subunit FeMo cofactor-binding domain.Semantic proximity Read ↗

Comparison of iron-molybdenum cofactor-deficient nitrogenase MoFe proteins by X-ray absorption spectroscopy: implications for P-cluster biosynthesis.Semantic proximity Read ↗

Heme biosynthesis is coupled to electron transport chains for energy generation.Semantic proximity Read ↗

ATP-independent substrate reduction by nitrogenase P-cluster variant.Semantic proximity Read ↗

P+ state of nitrogenase p-cluster exhibits electronic structure of a [Fe4S4]+ cluster.Semantic proximity Read ↗

The involvement of the nif-associated ferredoxin-like genes fdxA and fdxN of Herbaspirillum seropedicae in nitrogen fixation.Semantic proximity Read ↗

FeMo cofactor synthesis by a nifH mutant with altered MgATP reactivity.Semantic proximity Read ↗

Role for the nitrogenase MoFe protein alpha-subunit in FeMo-cofactor binding and catalysis.Semantic proximity Read ↗

Role of Escherichia coli nitrogen regulatory genes in the nitrogen response of the Azotobacter vinelandii NifL-NifA complex.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.