Evidence map›Paper›PMID 25037216›Full record

ArticleThe Journal of biological chemistry2014

Dynamics of the heme-binding bacterial gas-sensing dissimilative nitrate respiration regulator (DNR) and activation barriers for ligand binding and escape.

Laura Lobato, Latifa Bouzhir-Sima, Taku Yamashita, Michael T Wilson, Marten H Vos, Ursula Liebl

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Engineering a highly selective, hemoprotein-based scavenger as a carbon monoxide poisoning antidote with no hypertensive effect.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Early processes in heme-based CO-sensing proteins.Frontiers in molecular biosciences · 2022
    Review
  8. Article
  9. Article
  10. Bacterial Heme-Based Sensors of Nitric Oxide.Antioxidants & redox signaling · 2018
    Review
  11. Article
  12. Article
  13. Ultrafast photochemistry of the bcPhysical chemistry chemical physics : PCCP · 2017
    Article
  14. Review
  15. Review
  16. Article
  17. 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

6 authors at 3 institutions in 3 countries.

Laura LobatoLaboratory for Optics and Biosciences, CNRS, Ecole Polytechnique, 91128 Palaiseau, France,; INSERM U696, 91128 Palaiseau, France.
Latifa Bouzhir-SimaLaboratory for Optics and Biosciences, CNRS, Ecole Polytechnique, 91128 Palaiseau, France,; INSERM U696, 91128 Palaiseau, France.
Taku YamashitaLaboratory of Analytical Chemistry, Graduate School of Pharmaceutical Sciences, Osaka University, Yamadaoka, Suita, Osaka 565-0871, Japan, and.
Michael T WilsonSchool of Biological Sciences, University of Essex, Wivenhoe Park, Colchester C04 3SQ, United Kingdom.
Marten H VosLaboratory for Optics and Biosciences, CNRS, Ecole Polytechnique, 91128 Palaiseau, France,; INSERM U696, 91128 Palaiseau, France,. Electronic address: marten.vos@polytechnique.edu.
Ursula LieblLaboratory for Optics and Biosciences, CNRS, Ecole Polytechnique, 91128 Palaiseau, France,; INSERM U696, 91128 Palaiseau, France,. Electronic address: ursula.liebl@polytechnique.edu.
Centre National de la Recherche Scientifique · FROsaka University · JPUniversity of Essex · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNR (dissimilative nitrate respiration regulator) is a heme-binding transcription factor that is involved in the regulation of denitrification in Pseudomonas aeruginosa. In the ferrous deoxy state, the heme is 6-coordinate; external NO and CO can replace an internal ligand. Using fluorescence anisotropy, we show that high-affinity sequence-specific DNA binding occurs only when the heme is nitrosylated, consistent with the proposed function of DNR as NO sensor and transcriptional activator. This role is moreover supported by the NO "trapping" properties revealed by ultrafast spectroscopy that are similar to those of other heme-based NO sensor proteins. Dissociated CO-heme pairs rebind in an essentially barrierless way. This process competes with migration out of the heme pocket. The latter process is thermally activated (Ea ∼ 7 kJ/mol). This result is compared with other heme proteins, including the homologous CO sensor/transcription factor CooA, variants of the 5-coordinate mycobacterial sensor DosT and the electron transfer protein cytochrome c. This comparison indicates that thermal activation of ligand escape from the heme pocket is specific for systems where an external ligand replaces an internal one. The origin of this finding and possible implications are discussed.

Indexed as

AnimalsBacterial ProteinsBinding SitesCarbon MonoxideCytochromes cDNA, BacterialFluorescence PolarizationGene Expression Regulation, BacterialHemeHorsesKineticsLigandsNitric OxidePromoter Regions, GeneticProtein BindingPseudomonas aeruginosaBacterial ProteinsCarbon MonoxideCytochromes cDNA, BacterialDNR protein, Pseudomonas aeruginosaHemeLigandsNitric OxidenitrosylprotohemeTranscription FactorsCarbon MonoxideDNA Binding ProteinEnergeticsFluorescence AnisotropyHeme-based Sensor ProteinNitric OxideTranscription FactorUltrafast Spectroscopy

Identifiers

PMID25037216
PMCPMC4176248
OpenAlexW1974296775

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.