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

Hydrogenase activity in the foodborne pathogen Campylobacter jejuni depends upon a novel ABC-type nickel transporter (NikZYXWV) and is SlyD-independent.

Microbiology (Reading, England) - 1 Jun 2012

Howlett Robert M, Hughes Bethan M, Hitchcock Andrew, Kelly David J

Abstract excerpt

Campylobacter jejuni is a human pathogen of worldwide significance. It is commensal in the gut of many birds and mammals, where hydrogen is a readily available electron donor. The bacterium possesses a single membrane-bound, periplasmic-facing NiFe uptake hydrogenase that depends on the acquisition of environmental nickel for activity. The periplasmic binding protein Cj1584 (NikZ) of the ATP binding cassette...

Read the complete abstract on PubMed

Topics

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

Share to ATP-Binding Cassette Transporters
Share to Bacterial Proteins

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

Share to Biological Transport

Share to Campylobacter jejuni

Share to Foodborne Diseases

Share to Hydrogenase

Share to Nickel

Share to Peptidylprolyl Isomerase

Source

Identifiers

PMID: 22403188
DOI: 10.1099/mic.0.054130-0

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

Hydrogenase activity in the foodborne pathogen Campylobacter jejuni depends upon a novel ABC-type nickel transporter (NikZYXWV) and is SlyD-independent.PMID 22403188Read ↗

Nickel homeostasis in Escherichia coli - the rcnR-rcnA efflux pathway and its linkage to NikR function.Semantic proximity Read ↗

Comprehensive mapping of the Helicobacter pylori NikR regulon provides new insights in bacterial nickel responsesSemantic proximity Read ↗

A new insight into the role of intracellular nickel levels for the stress response, surface properties and twitching motility by Haemophilus influenzae.Semantic proximity Read ↗

Roles of the twin-arginine translocase and associated chaperones in the biogenesis of the electron transport chains of the human pathogen Campylobacter jejuni.Semantic proximity Read ↗

Helicobacter pylori HP1512 Is a Nickel-Responsive NikR-Regulated Outer Membrane ProteinSemantic proximity Read ↗

Rhizobium leguminosarum HupE is a highly-specific diffusion facilitator for nickel uptake.Semantic proximity Read ↗

NikR Mediates Nickel-Responsive Transcriptional Induction of Urease Expression in<i>Helicobacter pylori</i>Semantic proximity Read ↗

Structural and mechanistic insights into Helicobacter pylori NikR activation.Semantic proximity Read ↗

Characterization in Helicobacter pylori of a Nickel Transporter Essential for Colonization That Was Acquired during Evolution by Gastric Helicobacter SpeciesSemantic proximity Read ↗

Novel nickel transport mechanism across the bacterial outer membrane energized by the TonB/ExbB/ExbD machinery.Semantic proximity Read ↗

Uropathogenic enterobacteria use the yersiniabactin metallophore system to acquire nickelSemantic proximity Read ↗

The novel Helicobacter pylori CznABC metal efflux pump is required for cadmium, zinc, and nickel resistance, urease modulation, and gastric colonization.Semantic proximity Read ↗

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