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 glutathione in the formation of the active form of the oxygen sensor FNR ([4Fe-4S].FNR) and in the control of FNR function.

European journal of biochemistry - 1 Aug 2000

Tran Q H, Arras T, Becker S, Holighaus G, Ohlberger G, Unden G

Abstract excerpt

The oxygen sensor regulator FNR (fumarate nitrate reductase regulator) of Escherichia coli is known to be inactivated by O2 as the result of conversion of a [4Fe-4S] cluster of the protein into a [2Fe-2S] cluster. Further incubation with O2 causes loss of the [2Fe-2S] cluster and production of apoFNR. The reactions involved in cluster assembly and reductive activation of apoFNR isolated under anaerobic or aerobic...

Read the complete abstract on PubMed

Topics

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

Share to Dithiothreitol
Share to Glutaredoxins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glutathione

Share to Glutathione Reductase

Share to Iron-Sulfur Proteins

Share to Oxidoreductases

Share to Oxygen

Share to Spectrophotometry

Source

Identifiers

PMID: 10903516
DOI: 10.1046/j.1432-1327.2000.01539.x

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

Role of glutathione in the formation of the active form of the oxygen sensor FNR ([4Fe-4S].FNR) and in the control of FNR function.PMID 10903516Read ↗

DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen.Semantic proximity Read ↗

Substitution of leucine 28 with histidine in the Escherichia coli transcription factor FNR results in increased stability of the [4Fe-4S](2+) cluster to oxygen.Semantic proximity Read ↗

Regulation of aerobic-to-anaerobic transitions by the FNR cycle in Escherichia coli.Semantic proximity Read ↗

Covalently linking the Escherichia coli global anaerobic regulator FNR in tandem allows it to function as an oxygen stable dimer.Semantic proximity Read ↗

Nitric oxide formation by Escherichia coli. Dependence on nitrite reductase, the NO-sensing regulator Fnr, and flavohemoglobin Hmp.Semantic proximity Read ↗

Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways.Semantic proximity Read ↗

In vivo and in vitro mutants of FNR the anaerobic transcriptional regulator of E. coli.Semantic proximity Read ↗

The Transcriptional Repressor Protein NsrR Senses Nitric Oxide Directly via a [2Fe-2S] ClusterSemantic proximity Read ↗

Dissecting the role of the N-terminal region of the Escherichia coli global transcription factor FNR.Semantic proximity Read ↗

The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli.Semantic proximity Read ↗

Nitrosative stress in Escherichia coli: reduction of nitric oxide.Semantic proximity Read ↗

Repair of oxidized iron-sulfur clusters in Escherichia coli.Semantic proximity Read ↗

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