Evidence map›Paper›PMID 25576601›Full record

ArticleApplied and environmental microbiology2015

Arsenite oxidase also functions as an antimonite oxidase.

Qian Wang, Thomas P Warelow, Yoon-Suk Kang, Christine Romano, Thomas H Osborne, Corinne R Lehr, Brian Bothner, Timothy R McDermott, Joanne M Santini, Gejiao Wang

Erratum issuedAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Article
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  5. Review
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  7. Article
  8. Widespread Distribution of theEnvironmental science & technology · 2023
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  11. Nanozymes-Hitting the Biosensing "Target".Sensors (Basel, Switzerland) · 2021
    Review
  12. Review
  13. Article
  14. Article
  15. Functional mononuclear molybdenum enzymes: challenges and triumphs in molecular cloning, expression, and isolation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Qian WangState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan, People's Republic of China.
Thomas P WarelowInstitute of Structural & Molecular Biology, University College London, London, United Kingdom.
Yoon-Suk KangDepartment of Land Resources & Environmental Sciences, Montana State University, Bozeman, Montana, USA.
Christine RomanoDepartment of Land Resources & Environmental Sciences, Montana State University, Bozeman, Montana, USA.
Thomas H OsborneInstitute of Structural & Molecular Biology, University College London, London, United Kingdom.
Corinne R LehrChemistry & Biochemistry Department, California Polytechnic State University, San Luis Obispo, California, USA.
Brian BothnerDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, Montana, USA.
Timothy R McDermottDepartment of Land Resources & Environmental Sciences, Montana State University, Bozeman, Montana, USA.
Joanne M SantiniInstitute of Structural & Molecular Biology, University College London, London, United Kingdom j.santini@ucl.ac.uk gejiao@mail.hzau.edu.cn.
Gejiao WangState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan, People's Republic of China j.santini@ucl.ac.uk gejiao@mail.hzau.edu.cn.

Funding

Biotechnology and Biological Sciences Research Council BB/F016948/1
6 · The paper itself

Abstract

Arsenic and antimony are toxic metalloids and are considered priority environmental pollutants by the U.S. Environmental Protection Agency. Significant advances have been made in understanding microbe-arsenic interactions and how they influence arsenic redox speciation in the environment. However, even the most basic features of how and why a microorganism detects and reacts to antimony remain poorly understood. Previous work with Agrobacterium tumefaciens strain 5A concluded that oxidation of antimonite [Sb(III)] and arsenite [As(III)] required different biochemical pathways. Here, we show with in vivo experiments that a mutation in aioA [encoding the large subunit of As(III) oxidase] reduces the ability to oxidize Sb(III) by approximately one-third relative to the ability of the wild type. Further, in vitro studies with the purified As(III) oxidase from Rhizobium sp. strain NT-26 (AioA shares 94% amino acid sequence identity with AioA of A. tumefaciens) provide direct evidence of Sb(III) oxidation but also show a significantly decreased Vmax compared to that of As(III) oxidation. The aioBA genes encoding As(III) oxidase are induced by As(III) but not by Sb(III), whereas arsR gene expression is induced by both As(III) and Sb(III), suggesting that detection and transcriptional responses for As(III) and Sb(III) differ. While Sb(III) and As(III) are similar with respect to cellular extrusion (ArsB or Acr3) and interaction with ArsR, they differ in the regulatory mechanisms that control the expression of genes encoding the different Ars or Aio activities. In summary, this study documents an enzymatic basis for microbial Sb(III) oxidation, although additional Sb(III) oxidation activity also is apparent in this bacterium.

Indexed as

Agrobacterium tumefaciensAntimonyArsenitesOxidation-ReductionOxidoreductasesRhizobiumantimoniteAntimonyarsenitearsenite oxidaseArsenitesOxidoreductases

Identifiers

PMID25576601
PMCPMC4345363

What OpenQuestion holds

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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.