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

The induction of two biosynthetic enzymes helps Escherichia coli sustain heme synthesis and activate catalase during hydrogen peroxide stress.

Molecular microbiology - 1 May 2015

Mancini Stefano, Imlay James A

Abstract excerpt

Hydrogen peroxide pervades many natural environments, including the phagosomes that mediate cell-based immunity. Transcriptomic analysis showed that during protracted low-grade H(2)O(2) stress, Escherichia coli responds by activating both the OxyR defensive regulon and the Fur iron-starvation response. OxyR induced synthesis of two members of the nine-step heme biosynthetic pathway: ferrochelatase (HemH) and an...

Read the complete abstract on PubMed

Topics

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

Share to Biosynthetic Pathways
Share to Catalase
Share to Enzyme Induction

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

Share to Ferrochelatase

Share to Hydrogen Peroxide

Share to Porphyrins

Share to Regulon

Source

Open in PubMed Open full text

Identifiers

PMID: 25664592
DOI: 10.1111/mmi.12967
PMCID: PMC4430354

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

The induction of two biosynthetic enzymes helps Escherichia coli sustain heme synthesis and activate catalase during hydrogen peroxide stress.PMID 25664592Read ↗

Submicromolar hydrogen peroxide disrupts the ability of Fur protein to control free-iron levels in Escherichia coli.Semantic proximity Read ↗

Why do bacteria use so many enzymes to scavenge hydrogen peroxide?Semantic proximity Read ↗

Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx- mutants of Escherichia coli.Semantic proximity Read ↗

The YaaA protein of the Escherichia coli OxyR regulon lessens hydrogen peroxide toxicity by diminishing the amount of intracellular unincorporated iron.Semantic proximity Read ↗

Microarray analysis of Pseudomonas aeruginosa reveals induction of pyocin genes in response to hydrogen peroxideSemantic proximity Read ↗

Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes.Semantic proximity Read ↗

Escherichia coli deltafur mutant displays low HPII catalase activity in stationary phase.Semantic proximity Read ↗

Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrinSemantic proximity Read ↗

Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli.Semantic proximity Read ↗

OxyR Is a Convergent Target for Mutations Acquired during Adaptation to Oxidative Stress-Prone Metabolic States.Semantic proximity Read ↗

Mononuclear iron enzymes are primary targets of hydrogen peroxide stress.Semantic proximity Read ↗

Formate dehydrogenase, ubiquinone, and cytochrome bd-I are required for peptidoglycan recognition protein-induced oxidative stress and killing in Escherichia coli.Semantic proximity Read ↗

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