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 quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme.

Scientific reports - 26 Feb 2018

Gonska Nathalie, Young David, Yuki Riki, Okamoto Takuya, Hisano Tamao, Antonyuk Svetlana, Hasnain S Samar, Muramoto Kazumasa, Shiro Yoshitsugu, Tosha Takehiko, Ädelroth Pia

Abstract excerpt

Bacterial nitric oxide reductases (NORs) catalyse the reduction of NO to N2O and H2O. NORs are found either in denitrification chains, or in pathogens where their primary role is detoxification of NO produced by the immune defense of the host. Although NORs belong to the heme-copper oxidase superfamily, comprising proton-pumping O2-reducing enzymes, the best studied NORs, cNORs (cytochrome c-dependent), are...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Hemoglobin structure and function

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

Share to Mutation

Share to Neisseria meningitidis

Share to Nitric Oxide and Endothelin Effects

Share to Oxidoreductases

Share to Photosynthetic Processes and Mechanisms

Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 29483528
DOI: 10.1038/s41598-018-21804-0
PMCID: PMC5826923

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

Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme.PMID 29483528Read ↗

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

Exploring the terminal region of the proton pathway in the bacterial nitric oxide reductase.Semantic proximity Read ↗

The Functional Model Complex [Fe<sub>2</sub>(BPMP)(OPr)(NO)<sub>2</sub>](BPh<sub>4</sub>)<sub>2</sub> Provides Insight into the Mechanism of Flavodiiron NO ReductasesSemantic proximity Read ↗

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

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

New genes implicated in the protection of anaerobically grown Escherichia coli against nitric oxide.Semantic proximity Read ↗

Functional analysis of NsrR, a nitric oxide‐sensing Rrf2 repressor in Neisseria gonorrhoeaeSemantic proximity Read ↗

Superoxide reduction by Nanoarchaeum equitans neelaredoxin, an enzyme lacking the highly conserved glutamate iron ligand.Semantic proximity Read ↗

Bacterial Nitric-oxide Synthases Operate without a Dedicated Redox PartnerSemantic proximity Read ↗

Mutational and biochemical analysis of cytochrome c', a nitric oxide-binding lipoprotein important for adaptation of Neisseria gonorrhoeae to oxygen-limited growth.Semantic proximity Read ↗

Structural insights into the role of iron-histidine bond cleavage in nitric oxide-induced activation of H-NOX gas sensor proteins.Semantic proximity Read ↗

Diversity and complexity of flavodiiron NO/O2 reductases.Semantic proximity Read ↗

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