Evidence map›Paper›PMID 23818588›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Mn(II,III) oxidation and MnO2 mineralization by an expressed bacterial multicopper oxidase.

Cristina N Butterfield, Alexandra V Soldatova, Sung-Woo Lee, Thomas G Spiro, Bradley M Tebo

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. DistinguishingmSystems · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Redox-Driven Formation of Mn(III) in Ice.Environmental science & technology · 2024
    Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Distinguishing homogeneous advanced oxidation processes in bulk water from heterogeneous surface reactions in organic oxidation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Microbial functional diversity across biogeochemical provinces in the central Pacific Ocean.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Forced Biomineralization: A Review.Biomimetics (Basel, Switzerland) · 2021
    Review
  20. Synthesis of MnO/C/CoScience and technology of advanced materials · 2021
    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

5 authors.

Cristina N ButterfieldDivision of Environmental and Biomolecular Systems, Institute of Environmental Health, Oregon Health and Science University, Beaverton, OR 97006, USA.
Alexandra V Soldatova
Sung-Woo Lee
Thomas G Spiro
Bradley M Tebo

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reactive Mn(IV) oxide minerals are ubiquitous in the environment and control the bioavailability and distribution of many toxic and essential elements and organic compounds. Their formation is thought to be dependent on microbial enzymes, because spontaneous Mn(II) to Mn(IV) oxidation is slow. Several species of marine Bacillus spores oxidize Mn(II) on their exosporium, the outermost layer of the spore, encrusting them with Mn(IV) oxides. Molecular studies have identified the mnx (Mn oxidation) genes, including mnxG, encoding a putative multicopper oxidase (MCO), as responsible for this two-electron oxidation, a surprising finding because MCOs only catalyze single-electron transfer reactions. Characterization of the enzymatic mechanism has been hindered by the lack of purified protein. By purifying active protein from the mnxDEFG expression construct, we found that the resulting enzyme is a blue (absorption maximum 590 nm) complex containing MnxE, MnxF, and MnxG proteins. Further, by analyzing the Mn(II)- and (III)-oxidizing activity in the presence of a Mn(III) chelator, pyrophosphate, we found that the complex facilitates both electron transfers from Mn(II) to Mn(III) and from Mn(III) to Mn(IV). X-ray absorption spectroscopy of the Mn mineral product confirmed its similarity to Mn(IV) oxides generated by whole spores. Our results demonstrate that Mn oxidation from soluble Mn(II) to Mn(IV) oxides is a two-step reaction catalyzed by an MCO-containing complex. With the purification of active Mn oxidase, we will be able to uncover its mechanism, broadening our understanding of Mn mineral formation and the bioinorganic capabilities of MCOs.

Indexed as

BacillusCloning, MolecularDiphosphatesDNA PrimersEscherichia coliManganeseManganese CompoundsMass SpectrometryMultiprotein ComplexesOxidation-ReductionOxidesOxidoreductasesX-Ray Absorption Spectroscopycopper oxidaseDiphosphatesdiphosphoric acidDNA PrimersManganeseManganese Compoundsmanganese oxideMultiprotein ComplexesOxidesOxidoreductasesbiogeochemistrybiomineralizationmetal cyclingmicrobial redox

Identifiers

PMID23818588
PMCPMC3718108

What OpenQuestion holds

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Registered trials

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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.