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

Mapping the interaction of the [2Fe-2S] Clostridium pasteurianum ferredoxin with nitrogenase MoFe protein.

Biochimica et biophysica acta - 10 Sept 2001

Chatelet C, Meyer J

Abstract excerpt

The [2Fe-2S] ferredoxin from Clostridium pasteurianum had previously been shown to interact specifically with the nitrogenase MoFe protein, and electrostatic forces were found to be important contributors to the interaction. This phenomenon has now been analyzed in detail by using ferredoxin variants in which charge inversions or cancellations were introduced on all charged residues. The mutated forms of the...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Clostridium
Share to Cross-Linking Reagents

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electrophoresis, Polyacrylamide Gel

Share to Ferredoxins

Share to Nitrogenase

Share to Recombinant Proteins

Share to Static Electricity

Source

Identifiers

PMID: 11566366
DOI: 10.1016/s0167-4838(01)00246-1

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mapping the interaction of the [2Fe-2S] Clostridium pasteurianum ferredoxin with nitrogenase MoFe protein.PMID 11566366Read ↗

Cysteine ligand swapping on a deletable loop of the [2Fe-2S] ferredoxin from Clostridium pasteurianum.Semantic proximity Read ↗

Investigation of the role of surface residues in the ferredoxin from Clostridium pasteurianum.Semantic proximity Read ↗

Electrospray-ionization mass spectrometry of molecular variants of a [2Fe-2S] ferredoxin.Semantic proximity Read ↗

NMR study of the electron transfer complex of plant ferredoxin and sulfite reductase: mapping the interaction sites of ferredoxin.Semantic proximity Read ↗

Identification of residues of Rhodobacter capsulatus ferredoxin I important for its interaction with nitrogenase.Semantic proximity Read ↗

Site-specific mutagenesis of Rhodobacter capsulatus ferredoxin I, FdxN, that functions in nitrogen fixation. Role of extra residues.Semantic proximity Read ↗

High resolution crystal structures of the wild type and Cys-55-->Ser and Cys-59-->Ser variants of the thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus.Semantic proximity Read ↗

Involvement of the P cluster in intramolecular electron transfer within the nitrogenase MoFe protein.Semantic proximity Read ↗

Azotobacter vinelandii ferredoxin I: a sequence and structure comparison approach to alteration of [4Fe-4S]2+/+ reduction potential.Semantic proximity Read ↗

Alteration of the reduction potential of the [4Fe-4S](2+/+) cluster of Azotobacter vinelandii ferredoxin I.Semantic proximity Read ↗

The interaction of spinach nitrite reductase with ferredoxin: a site-directed mutation study.Semantic proximity Read ↗

Identification of the Ferredoxin-Binding Site of a Ferredoxin-Dependent Cyanobacterial Nitrate Reductase.Semantic proximity Read ↗

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