Evidence map›Paper›PMID 22198285›Full record

ReviewArchives of biochemistry and biophysics2012

Non-heme manganese catalase--the 'other' catalase.

James W Whittaker

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 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
–field-weighted citation impact
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

54 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Aqueous-stable Mn(II)-MOF nanoparticles with highJournal of materials chemistry. B · 2025
    Article
  7. OJournal of the American Chemical Society · 2025
    Article
  8. "mSphere · 2024
    Article
  9. Electron transfer in biological systems.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Review
  10. Article
  11. Review
  12. Article
  13. The Structural Biology of Catalase Evolution.Sub-cellular biochemistry · 2024
    Review
  14. Article
  15. Article
  16. Article
  17. Efficient Mn(II) removal mechanism byFrontiers in microbiology · 2023
    Article
  18. Monofunctional Heme-Catalases.Antioxidants (Basel, Switzerland) · 2022
    Review
  19. Article
  20. Catalysis and Electron Transfer inChemical reviews · 2022
    Review
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

1 author.

James W WhittakerInstitute for Environmental Health, Division of Environmental and Biomolecular Systems, Oregon Health and Science University, 20000 N.W. Walker Road, Beaverton, OR 97006-8921, USA. jim@ebs.ogi.edu

Funding

MANGANESE REDOX BIOCHEMISTRYR01GM042680 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI WHITTAKER, JAMES W · 1989 to 2012
$3.0M
NIGMS NIH HHS GM42680NIGMS NIH HHS R01 GM042680
6 · The paper itself

Abstract

Non-heme manganese catalases are widely distributed over microbial life and represent an environmentally important alternative to heme-containing catalases in antioxidant defense. Manganese catalases contain a binuclear manganese complex as their catalytic active site rather than a heme, and cycle between Mn(2)(II,II) and Mn(2)(III,III) states during turnover. X-ray crystallography has revealed the key structural elements of the binuclear manganese active site complex that can serve as the starting point for computational studies on the protein. Four manganese catalase enzymes have been isolated and characterized, and the enzyme appears to have a broad phylogenetic distribution including both bacteria and archae. More than 100 manganese catalase genes have been annotated in genomic databases, although the assignment of many of these putative manganese catalases needs to be experimentally verified. Iron limitation, exposure to low levels of peroxide stress, thermostability and cyanide resistance may provide the biological and environmental context for the occurrence of manganese catalases.

Indexed as

AntioxidantsBiochemistryCatalaseCatalytic DomainCrystallography, X-RayHemeLactiplantibacillus plantarumManganeseModels, ChemicalModels, MolecularMolecular ConformationOxidative StressPhylogenyReactive Oxygen SpeciesSolventsThermodynamicsAntioxidantsCatalaseHemeManganeseReactive Oxygen SpeciesSolvents

Identifiers

PMID22198285
PMCPMC3328634

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.