Evidence map›Paper›PMID 28159841›Full record

ArticleThe Journal of biological chemistry2017

Kinetic Mechanism of the Dechlorinating Flavin-dependent Monooxygenase HadA.

Panu Pimviriyakul, Kittisak Thotsaporn, Jeerus Sucharitakul, Pimchai Chaiyen

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

14 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Evolution of pollutant biodegradation.Applied microbiology and biotechnology · 2025
    Review
  3. Unlocking the catalytic precision of ligand-controlled enzymatic halogenation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Monooxygenation of aromatic compounds by flavin-dependent monooxygenases.Protein science : a publication of the Protein Society · 2019
    Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. 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 2 institutions in 1 country.

Panu PimviriyakulFrom the Department of Biochemistry and Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University, Bangkok 10400 and.
Kittisak Thotsapornthe Department of Biochemistry, Faculty of Dentistry, Chulalongkorn University, Bangkok 10300, Thailand.
Jeerus Sucharitakulthe Department of Biochemistry, Faculty of Dentistry, Chulalongkorn University, Bangkok 10300, Thailand.
Pimchai ChaiyenFrom the Department of Biochemistry and Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University, Bangkok 10400 and pimchai.cha@mahidol.ac.th.
Chulalongkorn University · THMahidol University · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The accumulation of chlorophenols (CPs) in the environment, due to their wide use as agrochemicals, has become a serious environmental problem. These organic halides can be degraded by aerobic microorganisms, where the initial steps of various biodegradation pathways include an oxidative dechlorinating process in which chloride is replaced by a hydroxyl substituent. Harnessing these dechlorinating processes could provide an opportunity for environmental remediation, but detailed catalytic mechanisms for these enzymes are not yet known. To close this gap, we now report transient kinetics and product analysis of the dechlorinating flavin-dependent monooxygenase, HadA, from the aerobic organism

Indexed as

ChlorophenolsFlavin-Adenine DinucleotideGram-Negative Bacterial InfectionsHalogenationHumansKineticsMixed Function OxygenasesRalstonia pickettiiSubstrate Specificitychlorophenol 4-monooxygenaseChlorophenolsFlavin-Adenine DinucleotideMixed Function Oxygenaseschlorophenolenzyme kineticsflavinflavin adenine dinucleotide (FAD)hydroxylasemonooxygenasepre-steady-state kinetics

Identifiers

PMID28159841
PMCPMC5377798
OpenAlexW2584691006

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.