Evidence map›Paper›PMID 23709220›Full record

ArticleThe Journal of biological chemistry2013

ubiI, a new gene in Escherichia coli coenzyme Q biosynthesis, is involved in aerobic C5-hydroxylation.

Mahmoud Hajj Chehade, Laurent Loiseau, Murielle Lombard, Ludovic Pecqueur, Alexandre Ismail, Myriam Smadja, Béatrice Golinelli-Pimpaneau, Caroline Mellot-Draznieks, Olivier Hamelin, Laurent Aussel and 5 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

33 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Understanding coenzyme Q.Physiological reviews · 2024
    Review
  5. An organic O donor for biological hydroxylation reactions.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Role of themBio · 2023
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. The EcoCyc Database in 2021.Frontiers in microbiology · 2021
    Article
  14. Coenzyme QFrontiers in bioengineering and biotechnology · 2021
    Article
  15. The OThe Journal of biological chemistry · 2020
    Article
  16. The Paradox of Coenzyme QNutrients · 2019
    Review
  17. Article
  18. Article
  19. A genome-wide screen inThe Journal of biological chemistry · 2017
    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

15 authors at 8 institutions in 1 country.

Mahmoud Hajj ChehadeCommissariat à l'Energie Atomique, Institut de Recherches en Technologies et Sciences pour le Vivant, Laboratoire Chimie et Biologie des Métaux, F-38054 Grenoble, France.
Laurent Loiseau
Murielle Lombard
Ludovic Pecqueur
Alexandre Ismail
Myriam Smadja
Béatrice Golinelli-Pimpaneau
Caroline Mellot-Draznieks
Olivier Hamelin
Laurent Aussel
Sylvie Kieffer-Jaquinod
Natty Labessan
Frédéric Barras
Marc Fontecave
Fabien Pierrel
Centre National de la Recherche Scientifique · FRAix-Marseille Université · FRCollège de France · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRInserm · FRInstitut de Microbiologie de la Méditerranée · FRInstitut de Recherches en Technologies et Sciences pour le Vivant · FRUniversité Joseph Fourier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coenzyme Q (ubiquinone or Q) is a redox-active lipid found in organisms ranging from bacteria to mammals in which it plays a crucial role in energy-generating processes. Q biosynthesis is a complex pathway that involves multiple proteins. In this work, we show that the uncharacterized conserved visC gene is involved in Q biosynthesis in Escherichia coli, and we have renamed it ubiI. Based on genetic and biochemical experiments, we establish that the UbiI protein functions in the C5-hydroxylation reaction. A strain deficient in ubiI has a low level of Q and accumulates a compound derived from the Q biosynthetic pathway, which we purified and characterized. We also demonstrate that UbiI is only implicated in aerobic Q biosynthesis and that an alternative enzyme catalyzes the C5-hydroxylation reaction in the absence of oxygen. We have solved the crystal structure of a truncated form of UbiI. This structure shares many features with the canonical FAD-dependent para-hydroxybenzoate hydroxylase and represents the first structural characterization of a monooxygenase involved in Q biosynthesis. Site-directed mutagenesis confirms that residues of the flavin binding pocket of UbiI are important for activity. With our identification of UbiI, the three monooxygenases necessary for aerobic Q biosynthesis in E. coli are known.

Indexed as

AerobiosisBinding SitesEscherichia coliEscherichia coli ProteinsFlavin-Adenine DinucleotideHydrolasesHydroxylationMixed Function OxygenasesMutagenesis, Site-DirectedUbiquinoneEscherichia coli ProteinsFlavin-Adenine DinucleotideHydrolasesMixed Function OxygenasesUbiI protein, E coliUbiquinoneCoenzyme QCrystal StructureEscherichia coliFlavinHydroxylaseMonooxygenaseubi Genes

Identifiers

PMID23709220
PMCPMC3707705
OpenAlexW1981179246

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.