Evidence map›Paper›PMID 25664592›Full record

ArticleMolecular microbiology2015

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

Stefano Mancini, James A Imlay

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.2field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

43 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
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  9. OxyR contributes to the oxidative stress capacity and virulence of hypervirulentFrontiers in cellular and infection microbiology · 2025
    Article
  10. Article
  11. Review
  12. Review
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  15. Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023
    Review
  16. Article
  17. Article
  18. Article
  19. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Stefano ManciniDepartment of Microbiology, University of Illinois, Urbana, IL, 61801, USA.
James A ImlayDepartment of Microbiology, University of Illinois, Urbana, IL, 61801, USA.
University of Illinois Urbana-Champaign · US

Funding

The Physiology of Oxidative Stress in Escherichia coliR01GM049640 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI IMLAY, JAMES A. · 1994 to 2024
$6.9M
The Physiology of Oxidative Stress in Escherichia coliR37GM049640 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI IMLAY, JAMES A. · 2007 to 2016
$5.3M
NIGMS NIH HHS GM49640NIGMS NIH HHS R01 GM049640NIGMS NIH HHS R37 GM049640
6 · The paper itself

Abstract

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 isozyme of coproporphyrinogen III oxidase (HemF). Mutations that blocked either adaptation caused the accumulation of porphyrin intermediates, inadequate activation of heme enzymes, low catalase activity, defective clearance of H(2)O(2) and a failure to grow. Genetic analysis indicated that HemH induction is needed to compensate for iron sequestration by the mini-ferritin Dps. Dps activity protects DNA and proteins by limiting Fenton chemistry, but it interferes with the ability of HemH to acquire the iron that it needs to complete heme synthesis. HemF is a manganoprotein that displaces HemN, an iron-sulfur enzyme whose synthesis and/or stability is apparently problematic during H(2)O(2) stress. Thus, the primary responses to H(2)O(2), including the sequestration of iron, require compensatory adjustments in the mechanisms of iron-cofactor synthesis. The results support the growing evidence that oxidative stress is primarily an iron pathology.

Indexed as

Oxidative StressBiosynthetic PathwaysCatalaseCoproporphyrinogen OxidaseEnzyme ActivationEnzyme InductionEscherichia coliEscherichia coli ProteinsFerrochelataseGene Expression ProfilingHemeHydrogen PeroxideMutationPorphyrinsRegulonRepressor ProteinsCatalaseCoproporphyrinogen OxidaseEscherichia coli ProteinsFerrochelataseHemeHydrogen PeroxideoxyR protein, E coliPorphyrinsRepressor Proteins

Identifiers

PMID25664592
PMCPMC4430354
OpenAlexW2110660474

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.