Evidence map›Paper›PMID 22609271›Full record

ReviewArchives of biochemistry and biophysics2012

Why do bacteria use so many enzymes to scavenge hydrogen peroxide?

Surabhi Mishra, James Imlay

Abstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 190 papers.

0numbers the graph read from it
0cells of the map it votes in
190citing papers in PubMed
19.6field-weighted citation impact, top 1% 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

190 citing papers in PubMed, 404 citations in OpenAlex.

  1. Article
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  4. Non-target influence of natural insecticide neem oil on bacterial growth and metabolism.International microbiology : the official journal of the Spanish Society for Microbiology · 2026
    Article
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  8. Detoxification of host-relevant HbioRxiv : the preprint server for biology · 2026
    Article
  9. Article
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  11. Factors governing the response ofFrontiers in cellular and infection microbiology · 2026
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

130 more citing papers are in PubMed but not listed here.

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.

Surabhi MishraDepartment of Microbiology, University of Illinois, Urbana, IL 61801, USA.
James Imlay
University of Illinois Urbana-Champaign · US

Funding

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 R37 GM049640
6 · The paper itself

Abstract

Hydrogen peroxide (H(2)O(2)) is continuously formed by the autoxidation of redox enzymes in aerobic cells, and it also enters from the environment, where it can be generated both by chemical processes and by the deliberate actions of competing organisms. Because H(2)O(2) is acutely toxic, bacteria elaborate scavenging enzymes to keep its intracellular concentration at nanomolar levels. Mutants that lack such enzymes grow poorly, suffer from high rates of mutagenesis, or even die. In order to understand how bacteria cope with oxidative stress, it is important to identify the key enzymes involved in H(2)O(2) degradation. Catalases and NADH peroxidase (Ahp) are primary scavengers in many bacteria, and their activities and physiological impacts have been unambiguously demonstrated through phenotypic analysis and through direct measurements of H(2)O(2) clearance in vivo. Yet a wide variety of additional enzymes have been proposed to serve similar roles: thiol peroxidase, bacterioferritin comigratory protein, glutathione peroxidase, cytochrome c peroxidase, and rubrerythrins. Each of these enzymes can degrade H(2)O(2) in vitro, but their contributions in vivo remain unclear. In this review we examine the genetic, genomic, regulatory, and biochemical evidence that each of these is a bonafide scavenger of H(2)O(2) in the cell. We also consider possible reasons that bacteria might require multiple enzymes to catalyze this process, including differences in substrate specificity, compartmentalization, cofactor requirements, kinetic optima, and enzyme stability. It is hoped that the resolution of these issues will lead to an understanding of stress resistance that is more accurate and perceptive.

Indexed as

Amino Acid SequenceBacteriaCatalaseCatalysisCytochrome-c PeroxidaseEscherichia coliHemeHemerythrinHydrogen PeroxideModels, ChemicalMolecular Sequence DataMutationOxidative StressPeroxidasesPhenotypePhotochemistryCatalaseCytochrome-c PeroxidaseHemeHemerythrinHydrogen PeroxideNAD+ peroxidasePeroxidasesRubredoxinsrubrerythrinsSulfhydryl Compounds

Identifiers

PMID22609271
PMCPMC3413786
OpenAlexW2058964632

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.