Evidence map›Paper›PMID 27030302›Full record

ArticleScientific reports2016

The Terminal Oxidase Cytochrome bd Promotes Sulfide-resistant Bacterial Respiration and Growth.

Elena Forte, Vitaliy B Borisov, Micol Falabella, Henrique G Colaço, Mariana Tinajero-Trejo, Robert K Poole, João B Vicente, Paolo Sarti, Alessandro Giuffrè

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 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
27.4field-weighted citation impact, top 1% 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

71 citing papers in PubMed, 138 citations in OpenAlex.

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  16. Membrane-Bound Redox Enzyme CytochromeInternational journal of molecular sciences · 2024
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11 more citing papers are in PubMed but not listed here.

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

9 authors at 8 institutions in 5 countries.

Elena ForteDepartment of Biochemical Sciences and Istituto Pasteur- Fondazione Cenci Bolognetti, Sapienza University of Rome, Italy.
Vitaliy B BorisovBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory, Moscow 119991, Russian Federation.
Micol FalabellaDepartment of Biochemical Sciences and Istituto Pasteur- Fondazione Cenci Bolognetti, Sapienza University of Rome, Italy.
Henrique G ColaçoMetabolism &Genetics Group, Research Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, University of Lisbon, Portugal.
Mariana Tinajero-TrejoCell Biology Program, The Hospital for Sick Children, Toronto, ON, Canada.
Robert K PooleDepartment of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield S10 2TN, United Kingdom.
João B VicenteInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.
Paolo SartiDepartment of Biochemical Sciences and Istituto Pasteur- Fondazione Cenci Bolognetti, Sapienza University of Rome, Italy.
Alessandro GiuffrèCNR Institute of Molecular Biology and Pathology, Rome, Italy.
Sapienza University of Rome · ITHospital for Sick Children · CAInstitute of Molecular Biology and Pathology · ITIstituto Pasteur · ITLomonosov Moscow State University · RUUniversidade Nova de Lisboa · PTUniversity of Lisbon · PTUniversity of Sheffield · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hydrogen sulfide (H2S) impairs mitochondrial respiration by potently inhibiting the heme-copper cytochrome c oxidase. Since many prokaryotes, including Escherichia (E.) coli, generate H2S and encounter high H2S levels particularly in the human gut, herein we tested whether bacteria can sustain sulfide-resistant O2-dependent respiration. E. coli has three respiratory oxidases, the cyanide-sensitive heme-copper bo3 enzyme and two bd oxidases much less sensitive to cyanide. Working on the isolated enzymes, we found that, whereas the bo3 oxidase is inhibited by sulfide with half-maximal inhibitory concentration IC50 = 1.1 ± 0.1 μM, under identical experimental conditions both bd oxidases are insensitive to sulfide up to 58 μM. In E. coli respiratory mutants, both O2-consumption and aerobic growth proved to be severely impaired by sulfide when respiration was sustained by the bo3 oxidase alone, but unaffected by ≤200 μM sulfide when either bd enzyme acted as the only terminal oxidase. Accordingly, wild-type E. coli showed sulfide-insensitive respiration and growth under conditions favouring the expression of bd oxidases. In all tested conditions, cyanide mimicked the functional effect of sulfide on bacterial respiration. We conclude that bd oxidases promote sulfide-resistant O2-consumption and growth in E. coli and possibly other bacteria. The impact of this discovery is discussed.

Indexed as

Gene Expression Regulation, BacterialAerobiosisCyanidesCytochrome b GroupCytochromesElectron Transport Chain Complex ProteinsEscherichia coliEscherichia coli ProteinsHydrogen SulfideIsoenzymesKineticsOxidoreductasesOxygenCyanidescytochrome bd terminal oxidase complex, E coliCytochrome b Groupcytochrome bo3, E coliCytochromesElectron Transport Chain Complex ProteinsEscherichia coli ProteinsHydrogen SulfideIsoenzymesOxidoreductasesOxygen

Identifiers

PMID27030302
PMCPMC4815019
OpenAlexW2333057557

What OpenQuestion holds

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LicenceCC BY
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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.