Evidence map›Paper›PMID 22380602›Full record

ArticleBMC microbiology2012

Identification of the para-nitrophenol catabolic pathway, and characterization of three enzymes involved in the hydroquinone pathway, in Peudomonas sp. 1-7.

Shuangyu Zhang, Wen Sun, Li Xu, Xiaomei Zheng, Xiaoyu Chu, Jian Tian, Ningfeng Wu, Yunliu Fan

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

26 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Characterization of the substrate specificity and regioselectivity of ring-cleavage of Pseudomonas putida DLL-E4 hydroquinone 1,2-dioxygenase (PnpC1C2).Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Article
  3. Biodegradation mechanisms ofFrontiers in microbiology · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Transcriptomic analysis of Burkholderia cenocepacia CEIB S5-2 during methyl parathion degradation.Environmental science and pollution research international · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

8 authors at 2 institutions in 1 country.

Shuangyu ZhangBiotechnology Research Institute, Chinese Academy of Agricultural Sciences, Haidian District, Beijing 100081, PR China.
Wen Sun
Li Xu
Xiaomei Zheng
Xiaoyu Chu
Jian Tian
Ningfeng Wu
Yunliu Fan
Chinese Academy of Agricultural Sciences · CNBiotechnology Research Institute · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundpara-Nitrophenol (PNP), a priority environmental pollutant, is hazardous to humans and animals. However, the information relating to the PNP degradation pathways and their enzymes remain limited.

resultsPseudomonas sp.1-7 was isolated from methyl parathion (MP)-polluted activated sludge and was shown to degrade PNP. Two different intermediates, hydroquinone (HQ) and 4-nitrocatechol (4-NC) were detected in the catabolism of PNP. This indicated that Pseudomonas sp.1-7 degraded PNP by two different pathways, namely the HQ pathway, and the hydroxyquinol (BT) pathway (also referred to as the 4-NC pathway). A gene cluster (pdcEDGFCBA) was identified in a 10.6 kb DNA fragment of a fosmid library, which cluster encoded the following enzymes involved in PNP degradation: PNP 4-monooxygenase (PdcA), p-benzoquinone (BQ) reductase (PdcB), hydroxyquinol (BT) 1,2-dioxygenase (PdcC), maleylacetate (MA) reductase (PdcF), 4-hydroxymuconic semialdehyde (4-HS) dehydrogenase (PdcG), and hydroquinone (HQ) 1,2-dioxygenase (PdcDE). Four genes (pdcDEFG) were expressed in E. coli and the purified pdcDE, pdcG and pdcF gene products were shown to convert HQ to 4-HS, 4-HS to MA and MA to β-ketoadipate respectively by in vitro activity assays.

conclusionsThe cloning, sequencing, and characterization of these genes along with the functional PNP degradation studies identified 4-NC, HQ, 4-HS, and MA as intermediates in the degradation pathway of PNP by Pseudomonas sp.1-7. This is the first conclusive report for both 4-NC and HQ- mediated degradation of PNP by one microorganism.

Indexed as

Bacterial ProteinsChromatography, LiquidEnvironmental PollutantsEscherichia coliGene OrderHydroquinonesMass SpectrometryMolecular Sequence DataMultigene FamilyNitrophenolsOxidoreductasesPseudomonasBacterial ProteinsEnvironmental PollutantsHydroquinonesNitrophenolsOxidoreductases

Identifiers

PMID22380602
PMCPMC3324391
OpenAlexW2065068621

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.