Evidence map›Paper›PMID 36406263›Full record

ReviewFrontiers in molecular biosciences2022

Early processes in heme-based CO-sensing proteins.

Marten H Vos, Mayla Salman, Ursula Liebl

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Carbon Monoxide and Prokaryotic Energy Metabolism.International journal of molecular sciences · 2025
    Review
  2. 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

3 authors.

Marten H VosLaboratoire d'Optique et Biosciences, Centre National de la Recherche Scientifique, Institut National de la Santé et de la Recherche Médicale, École Polytechnique, Institut Polytechnique de Paris, Paris, France.
Mayla SalmanLaboratoire d'Optique et Biosciences, Centre National de la Recherche Scientifique, Institut National de la Santé et de la Recherche Médicale, École Polytechnique, Institut Polytechnique de Paris, Paris, France.
Ursula LieblLaboratoire d'Optique et Biosciences, Centre National de la Recherche Scientifique, Institut National de la Santé et de la Recherche Médicale, École Polytechnique, Institut Polytechnique de Paris, Paris, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbon monoxide has been recognized relatively recently as signaling molecule, and only very few dedicated natural CO sensor proteins have been identified so far. These include in particular heme-based transcription factors: the bacterial sensor proteins CooA and RcoM. In these 6-coordinated systems, exchange between an internal protein residue and CO as a heme ligand in the sensor domain affects the properties of the DNA-binding domain. Using light to dissociate heme-ligand bonds can in principle initiate this switching process. We review the efforts to use this method to investigate early processes in ligand switching and signaling, with an emphasis on the CO-"trappingˮ properties of the heme cavity. These features are unusual for most heme proteins, but common for heme-based CO sensors.

Indexed as

carbon monoxideCooAhemeligand dynamicsRcoMsensor proteinultrafast spectroscopy

Identifiers

PMID36406263
PMCPMC9670170

What OpenQuestion holds

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Registered trials

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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.