Evidence map›Paper›PMID 21906340›Full record

ArticleAMB Express2011

Purification and characterization of hydroquinone dioxygenase from Sphingomonas sp. strain TTNP3.

Boris A Kolvenbach, Markus Lenz, Dirk Benndorf, Erdmann Rapp, Jan Fousek, Cestmir Vlcek, Andreas Schäffer, Frédéric Lp Gabriel, Hans-Peter E Kohler, Philippe Fx Corvini

Open access · goldAbstract read
In one paragraph

Article in AMB Express, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

15 citing papers in PubMed, 35 citations in OpenAlex.

  1. 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
  2. Metabolic mechanism of lignin-derived aromatics in white-rot fungi.Applied microbiology and biotechnology · 2024
    Review
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  13. Crystallization and preliminary X-ray crystallographic analysis of hydroquinone dioxygenase from Sphingomonas sp. TTNP3.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
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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

10 authors at 8 institutions in 5 countries.

Boris A KolvenbachInstitute for Ecopreneurship, School of Life Sciences, University of Applied Sciences Northwestern Switzerland, Muttenz, Switzerland. boris.kolvenbach@fhnw.ch.
Markus Lenz
Dirk Benndorf
Erdmann Rapp
Jan Fousek
Cestmir Vlcek
Andreas Schäffer
Frédéric Lp Gabriel
Hans-Peter E Kohler
Philippe Fx Corvini
FHNW University of Applied Sciences and Arts · CHCzech Academy of Sciences · CZCzech Academy of Sciences, Institute of Molecular Genetics · CZMax Planck Institute for Dynamics of Complex Technical Systems · DEOtto-von-Guericke University Magdeburg · DERWTH Aachen University · DESwiss Federal Institute of Aquatic Science and Technology · CHUniversity of Rostock · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hydroquinone-1,2-dioxygenase, an enzyme involved in the degradation of alkylphenols in Sphingomonas sp. strain TTNP3 was purified to apparent homogeneity. The extradiol dioxygenase catalyzed the ring fission of hydroquinone to 4-hydroxymuconic semialdehyde and the degradation of chlorinated and several alkylated hydroquinones. The activity of 1 mg of the purified enzyme with unsubstituted hydroquinone was 6.1 μmol per minute, the apparent Km 2.2 μM. ICP-MS analysis revealed an iron content of 1.4 moles per mole enzyme. The enzyme lost activity upon exposure to oxygen, but could be reactivated by Fe(II) in presence of ascorbate. SDS-PAGE analysis of the purified enzyme yielded two bands of an apparent size of 38 kDa and 19 kDa, respectively. Data from MALDI-TOF analyses of peptides of the respective bands matched with the deduced amino acid sequences of two neighboring open reading frames found in genomic DNA of Sphingomonas sp strain TTNP3. The deduced amino acid sequences showed 62% and 47% identity to the large and small subunit of hydroquinone dioxygenase from Pseudomonas fluorescens strain ACB, respectively. This heterotetrameric enzyme is the first of its kind found in a strain of the genus Sphingomonas sensu latu.

Identifiers

PMID21906340
PMCPMC3222310
OpenAlexW2156780427

What OpenQuestion holds

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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.