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

Diversity and complexity of flavodiiron NO/O2 reductases.

FEMS microbiology letters - 1 Feb 2018

Folgosa Filipe, Martins Maria C, Teixeira Miguel

Abstract excerpt

Flavodiiron proteins (FDPs) are a family of enzymes endowed with nitric oxide (NO) or oxygen reductase activities, forming the innocuous nitrous oxide (N2O) or water molecules, respectively. FDPs are widespread in the three life kingdoms, and have a modular nature, being each monomer minimally constituted by a metallo-β-lactamase-like domain containing a catalytic diiron centre, followed by a flavodoxin one, with...

Read the complete abstract on PubMed

Topics

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

Share to Protein Domains
Share to Catalysis
Share to Electron-Transferring Flavoproteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Flavins

Share to Nitric Oxide

Share to Oxidoreductases

Share to Oxygen

Source

Identifiers

PMID: 29240952
DOI: 10.1093/femsle/fnx267

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Diversity and complexity of flavodiiron NO/O2 reductases.PMID 29240952Read ↗

The multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductaseSemantic proximity Read ↗

Nitric oxide dioxygenase: an enzymic function for flavohemoglobin.Semantic proximity Read ↗

Evolution of the haem copper oxidases superfamily: a rooting tale.Semantic proximity Read ↗

Histidine ligand variants of a flavo-diiron protein: effects on structure and activities.Semantic proximity Read ↗

Phylogenetic analysis reveals the surprising diversity of an oxygenase class.Semantic proximity Read ↗

Flavodiiron oxygen reductase from Entamoeba histolytica: modulation of substrate preference by tyrosine 271 and lysine 53.Semantic proximity Read ↗

Mn/Fe superoxide dismutase interaction fingerprints and prediction of oligomerization and metal cofactor from sequence.Semantic proximity Read ↗

Structure-function studies of the quinol dependent Nitric Oxide Reductase (qNOR) from Alcaligenes xylosoxidansSemantic proximity Read ↗

Co-Occurrence of Enzyme Domains Guides the Discovery of an Oxazolone SynthetaseSemantic proximity Read ↗

Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme.Semantic proximity Read ↗

Flavorubredoxin, an inducible catalyst for nitric oxide reduction and detoxification in Escherichia coli.Semantic proximity Read ↗

Large-scale examination of functional and sequence diversity of 2-oxoglutarate/Fe(II)-dependent oxygenases in Metazoa.Semantic proximity Read ↗

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