Evidence map›Paper›PMID 27279363›Full record

ArticleScientific reports2016

Cytochrome bd Displays Significant Quinol Peroxidase Activity.

Sinan Al-Attar, Yuanjie Yu, Martijn Pinkse, Jo Hoeser, Thorsten Friedrich, Dirk Bald, Simon de Vries

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

43 citing papers in PubMed, 81 citations in OpenAlex.

  1. Aerotolerant capacity of the lung symbiontJournal of bacteriology · 2026
    Article
  2. Review
  3. The Crucial Role of LTTR_0390 inJournal of agricultural and food chemistry · 2026
    Article
  4. A cytochromeApplied and environmental microbiology · 2025
    Article
  5. Article
  6. Article
  7. Membrane-Bound Redox Enzyme CytochromeInternational journal of molecular sciences · 2024
    Article
  8. The respiratory chain ofFrontiers in microbiology · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Bioenergetics and Reactive Nitrogen Species in Bacteria.International journal of molecular sciences · 2022
    Review
  13. Review
  14. Recent Advances in Structural Studies of CytochromeInternational journal of molecular sciences · 2022
    Review
  15. Article
  16. Impact of Hydrogen Sulfide on Mitochondrial and Bacterial Bioenergetics.International journal of molecular sciences · 2021
    Review
  17. Article
  18. Review
  19. Review
  20. Bacterial Oxidases of the CytochromeAntioxidants & redox signaling · 2021
    Review
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

7 authors at 2 institutions in 2 countries.

Sinan Al-AttarDepartment of Biotechnology, Delft University of Technology, The Netherlands.
Yuanjie YuDepartment of Biotechnology, Delft University of Technology, The Netherlands.
Martijn PinkseDepartment of Biotechnology, Delft University of Technology, The Netherlands.
Jo HoeserInstitut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstr 21, 79014 Freiburg i. Br., Germany.
Thorsten FriedrichInstitut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstr 21, 79014 Freiburg i. Br., Germany.
Dirk BaldDepartment of Molecular Cell Biology, AIMMS, Faculty of Earth- and Life Sciences, VU University Amsterdam, Amsterdam, The Netherlands.
Simon de VriesDepartment of Biotechnology, Delft University of Technology, The Netherlands.
Delft University of Technology · NLUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytochrome bd is a prokaryotic terminal oxidase that catalyses the electrogenic reduction of oxygen to water using ubiquinol as electron donor. Cytochrome bd is a tri-haem integral membrane enzyme carrying a low-spin haem b558, and two high-spin haems: b595 and d. Here we show that besides its oxidase activity, cytochrome bd from Escherichia coli is a genuine quinol peroxidase (QPO) that reduces hydrogen peroxide to water. The highly active and pure enzyme preparation used in this study did not display the catalase activity recently reported for E. coli cytochrome bd. To our knowledge, cytochrome bd is the first membrane-bound quinol peroxidase detected in E. coli. The observation that cytochrome bd is a quinol peroxidase, can provide a biochemical basis for its role in detoxification of hydrogen peroxide and may explain the frequent findings reported in the literature that indicate increased sensitivity to hydrogen peroxide and decreased virulence in mutants that lack the enzyme.

Indexed as

Cytochrome b GroupCytochromesElectron Transport Chain Complex ProteinsEscherichia coli ProteinsHydroquinonesKineticsOxidoreductasesSubstrate Specificitycytochrome bd terminal oxidase complex, E coliCytochrome b GroupCytochromesElectron Transport Chain Complex ProteinsEscherichia coli ProteinsHydroquinonesOxidoreductases

Identifiers

PMID27279363
PMCPMC4899803
OpenAlexW2416291335

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.