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

Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans.

Archives of biochemistry and biophysics - 1 Mar 2009

Sedlácek Vojtech, van Spanning Rob J M, Kucera Igor

Abstract excerpt

The ferric reductase B (FerB) protein of Paracoccus denitrificans exhibits activity of an NAD(P)H: Fe(III) chelate, chromate and quinone oxidoreductase. Sequence analysis places FerB in a family of soluble flavin-containing quinone reductases. The enzyme reduces a range of quinone substrates, inc...

Read the complete abstract on PubMed

Topics

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

Share to Enzyme Inhibitors
Share to FMN Reductase
Share to Genes, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to NAD(P)H Dehydrogenase (Quinone)

Share to Paracoccus denitrificans

Share to Quinones

Share to Recombinant Fusion Proteins

Share to Substrate Specificity

Source

Identifiers

PMID: 19138657
DOI: 10.1016/j.abb.2008.12.016

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19138657-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans.PMID 19138657Read ↗

Ferric reductase A is essential for effective iron acquisition in Paracoccus denitrificans.Semantic proximity Read ↗

Proteomic responses to a methyl viologen-induced oxidative stress in the wild type and FerB mutant strains of Paracoccus denitrificans.Semantic proximity Read ↗

Expression and characterization of a functional canine variant of cytochrome b5 reductase.Semantic proximity Read ↗

Global transcriptional response of Caulobacter crescentus to iron availability.Semantic proximity Read ↗

The cytochrome bc complex (menaquinone:cytochrome c reductase) in Bacillus subtilis has a nontraditional subunit organization.Semantic proximity Read ↗

Ferredoxin-NADP+ reductase from Pseudomonas putida functions as a ferric reductase.Semantic proximity Read ↗

Paracoccus denitrificans cytochrome c1 gene replacement mutants.Semantic proximity Read ↗

Electron transfer in Paracoccus denitrificans with the modified fbc operon.Semantic proximity Read ↗

Isolation and characterization of a thermostable F420:NADPH oxidoreductase from Thermobifida fusca.Semantic proximity Read ↗

Characterization of a nif-regulated flavoprotein (FprA) from Rhodobacter capsulatus. Redox properties and molecular interaction with a [2Fe-2S] ferredoxin.Semantic proximity Read ↗

Mutagenesis of the gene encoding cytochrome c550 of Paracoccus denitrificans and analysis of the resultant physiological effects.Semantic proximity Read ↗

The cbb3-type cytochrome c oxidase from Rhodobacter sphaeroides, a proton-pumping heme-copper oxidase.Semantic proximity Read ↗

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