Evidence map›Paper›PMID 18165363›Full record

ArticleApplied and environmental microbiology2008

Direct identification of a bacterial manganese(II) oxidase, the multicopper oxidase MnxG, from spores of several different marine Bacillus species.

Gregory J Dick, Justin W Torpey, Terry J Beveridge, Bradley M Tebo

Abstract readComparative Study
In one paragraph

Article in Applied and environmental microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
12.7field-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

55 citing papers in PubMed, 160 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Changes in the Microbiome of Sugarcane (Life (Basel, Switzerland) · 2023
    Article
  7. Article
  8. A halophilicFrontiers in microbiology · 2023
    Article
  9. Review
  10. Article
  11. Article
  12. Genes · 2022
    Article
  13. Proteomic insights into Lysinibacillus sp.-mediated biosolubilization of manganese.Environmental science and pollution research international · 2021
    Article
  14. Article
  15. Review
  16. Manganese Stress Adaptation Mechanisms ofFrontiers in microbiology · 2021
    Article
  17. Article
  18. Manganese (II) removal from aqueous solutions byBiotechnology reports (Amsterdam, Netherlands) · 2020
    Article
  19. Mn(III) species formed by the multi-copper oxidase MnxG investigated by electron paramagnetic resonance spectroscopy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Article
  20. 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 3 institutions in 2 countries.

Gregory J DickMarine Biology Research Division, Scripps Institution of Oceanography, University of California San Diego, 9500 Gilman Drive, La Jolla, California 92093-02021, USA.
Justin W Torpey
Terry J Beveridge
Bradley M Tebo
Scripps Institution of Oceanography · USUniversity of California, San Diego · USUniversity of Guelph · CA

Funding

Yeast Genetics and Stress Response Genes-BiomedicalP42ES010337 · NIEHS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TUKEY, ROBERT H · 2000 to 2022
$69.8M
NIEHS NIH HHS ES10337NIEHS NIH HHS P42 ES010337
6 · The paper itself

Abstract

Microorganisms catalyze the formation of naturally occurring Mn oxides, but little is known about the biochemical mechanisms of this important biogeochemical process. We used tandem mass spectrometry to directly analyze the Mn(II)-oxidizing enzyme from marine Bacillus spores, identified as an Mn oxide band with an in-gel activity assay. Nine distinct peptides recovered from the Mn oxide band of two Bacillus species were unique to the multicopper oxidase MnxG, and one peptide was from the small hydrophobic protein MnxF. No other proteins were detected in the Mn oxide band, indicating that MnxG (or a MnxF/G complex) directly catalyzes biogenic Mn oxide formation. The Mn(II) oxidase was partially purified and found to be resistant to many proteases and active even at high concentrations of sodium dodecyl sulfate. Comparative analysis of the genes involved in Mn(II) oxidation from three diverse Bacillus species revealed a complement of conserved Cu-binding regions not present in well-characterized multicopper oxidases. Our results provide the first direct identification of a bacterial enzyme that catalyzes Mn(II) oxidation and suggest that MnxG catalyzes two sequential one-electron oxidations from Mn(II) to Mn(III) and from Mn(III) to Mn(IV), a novel type of reaction for a multicopper oxidase.

Indexed as

BacillusBase SequenceCopperElectrophoresis, Polyacrylamide GelManganeseMarine BiologyMicroscopy, Electron, TransmissionMolecular Sequence DataOxidation-ReductionOxidoreductasesSequence Analysis, DNASpores, BacterialTandem Mass SpectrometryWater MicrobiologyCopperManganeseOxidoreductases

Identifiers

PMID18165363
PMCPMC2258647
OpenAlexW2106633126

What OpenQuestion holds

Textmetadata
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.