Evidence map›Paper›PMID 26991114›Full record

ArticleMolecular microbiology2016

The cytochrome bd oxidase of Escherichia coli prevents respiratory inhibition by endogenous and exogenous hydrogen sulfide.

Sergey Korshunov, Karin R C Imlay, James A Imlay

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
7.2field-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

60 citing papers in PubMed, 96 citations in OpenAlex.

  1. Review
  2. Self-bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. A cytochromeApplied and environmental microbiology · 2025
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  7. Article
  8. Insights from a Genome-Wide Study ofCurrent issues in molecular biology · 2025
    Article
  9. Effect of HArchives of microbiology · 2024
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  10. Article
  11. Article
  12. Regulation of Cysteine Homeostasis and Its Effect onInternational journal of molecular sciences · 2024
    Article
  13. Membrane-Bound Redox Enzyme CytochromeInternational journal of molecular sciences · 2024
    Article
  14. Article
  15. Article
  16. Cysteine Biosynthesis inBiomolecules · 2022
    Article
  17. Review
  18. Article
  19. The Sulfide-Responsive SqrR/BigR Homologous Regulator YgaV ofAntioxidants (Basel, Switzerland) · 2022
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Sergey KorshunovDepartment of Microbiology, University of Illinois, Urbana, IL, 61801, USA.
Karin R C ImlayDepartment of Microbiology, University of Illinois, Urbana, IL, 61801, USA.
James A ImlayDepartment of Microbiology, University of Illinois, Urbana, IL, 61801, USA.
University of Illinois Urbana-Champaign · US

Funding

Soft Metal, Disulfide, and Cysteine Stresses in Escherichia coliR01GM101012 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI IMLAY, JAMES A. · 2012 to 2020
$2.2M
NIGMS NIH HHS R01 GM101012
6 · The paper itself

Abstract

When sulfur compounds are scarce or difficult to process, Escherichia coli adapts by inducing the high-level expression of sulfur-compound importers. If cystine then becomes available, the cystine is rapidly overimported and reduced, leading to a burgeoning pool of intracellular cysteine. Most of the excess cysteine is exported, but some is adventitiously degraded, with the consequent release of sulfide. Sulfide is a potent ligand of copper and heme moieties, raising the prospect that it interferes with enzymes. We observed that when cystine was provided and sulfide levels rose, E. coli became strictly dependent upon cytochrome bd oxidase for continued respiration. Inspection revealed that low-micromolar levels of sulfide inhibited the proton-pumping cytochrome bo oxidase that is regarded as the primary respiratory oxidase. In the absence of the back-up cytochrome bd oxidase, growth failed. Exogenous sulfide elicited the same effect. The potency of sulfide was enhanced when oxygen concentrations were low. Natural oxic-anoxic interfaces are often sulfidic, including the intestinal environment where E. coli dwells. We propose that the sulfide resistance of the cytochrome bd oxidase is a key trait that permits respiration in such habitats.

Indexed as

Cytochrome b GroupCytochromesElectron Transport Chain Complex ProteinsElectron Transport Complex IVEscherichia coliEscherichia coli ProteinsHydrogen SulfideOxidoreductasesOxygenOxygen Consumptioncytochrome bd terminal oxidase complex, E coliCytochrome b Groupcytochrome o oxidaseCytochromesElectron Transport Chain Complex ProteinsElectron Transport Complex IVEscherichia coli ProteinsHydrogen SulfideOxidoreductasesOxygen

Identifiers

PMID26991114
PMCPMC4925259
OpenAlexW2299156747

What OpenQuestion holds

Textmetadata
LicenceTDM
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.