Evidence map›Paper›PMID 25964067›Full record

ArticleBiochimica et biophysica acta2015

Iron incorporation into MnSOD A (bacterial Mn-dependent superoxide dismutase) leads to the formation of a peroxidase/catalase implicated in oxidative damage to bacteria.

Douglas Ganini, Robert M Petrovich, Lori L Edwards, Ronald P Mason

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.0field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. The curious life of human mitochondrial SOD2.International journal of biological macromolecules · 2026
    Review
  4. Article
  5. Article
  6. Article
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  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Insights into the Dichotomous Regulation of SOD2 in Cancer.Antioxidants (Basel, Switzerland) · 2017
    Review
  16. Review
  17. Article
  18. Article
  19. Article
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

4 authors at 1 institution in 1 country.

Douglas GaniniFree Radical Metabolites Group, Immunity, Inflammation & Disease Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA. Electronic address: ganinidasilvad@niehs.nih.gov.
Robert M PetrovichProtein Expression Core Facility, Genome Integrity & Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA.
Lori L EdwardsProtein Expression Core Facility, Genome Integrity & Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA.
Ronald P MasonFree Radical Metabolites Group, Immunity, Inflammation & Disease Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA.
National Institute of Environmental Health Sciences · US

Funding

Protein Expression FacilityZICES102487 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI PETROVICH, ROBERT · 2009 to 2025
$23.9M
Protein Derived RadicalsZIAES050139 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI MASON, RONALD P · 2009 to 2018
$17.5M
Intramural NIH HHS Z99 ES999999Intramural NIH HHS ZIA ES050139Intramural NIH HHS ZIC ES102487
6 · The paper itself

Abstract

backgroundMn/Fe-superoxide dismutase (SOD) is a family of enzymes essential for organisms to be able to cope with oxygen. These enzymes bound to their classical metals catalyze the dismutation of the free radical superoxide anion (O2(-)) to H2O2 and molecular oxygen. E. coli has the manganese-dependent SOD A and the iron-dependent SOD B.

methodsStrains of E. coli overexpressing SOD A or SOD B were grown in media with different metal compositions. SODs were purified and their metal content and SOD activity were determined. Those proteins were incubated with H2O2 and assayed for oxidation of Amplex red or o-phenylenediamine, consumption of H2O2, release of iron and protein radical formation. Cell survival was determined in bacteria with MnSOD A or FeSOD A after being challenged with H2O2.

resultsWe show for the first time that the bacterial manganese-dependent SOD A when bound to iron (FeSOD A) has peroxidase activity. The in vivo formation of the peroxidase FeSOD A was increased when media had higher levels of iron because of a decreased manganese metal incorporation. In comparison to bacteria with MnSOD A, cells with FeSOD A had a higher loss of viability when exposed to H2O2. GENERAL SIGNIFICANCE: The biological occurrence of this fundamental antioxidant enzyme in an alternative iron-dependent state represents an important source of free radical formation.

Indexed as

BacteriaBacterial ProteinsCatalaseIronPeroxidaseSuperoxide DismutaseBacterial ProteinsCatalaseIronPeroxidaseSodA protein, BacteriaSodB protein, BacteriaSuperoxide DismutaseFree radicalIronManganeseMetalPeroxidaseSuperoxide dismutase (SOD)

Identifiers

PMID25964067
PMCPMC4516619
OpenAlexW761534969

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.