Evidence map›Paper›PMID 22494151›Full record

ReviewAntioxidants & redox signaling2012

Environmental heme-based sensor proteins: implications for understanding bacterial pathogenesis.

Aisha Farhana, Vikram Saini, Ashwani Kumar, Jack R Lancaster, Adrie J C Steyn

Open access · greenAbstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 49 citations in OpenAlex.

  1. Structural Basis of a Novel Heme Binding Bacterial One-Component Switch.bioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Multistep Signaling in Nature: A Close-Up ofInternational journal of molecular sciences · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Chemical foundations of hydrogen sulfide biology.Nitric oxide : biology and chemistry · 2013
    Review
  15. Review
  16. Review
  17. Heme sensor proteins.The Journal of biological chemistry · 2013
    Review
  18. 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

5 authors at 2 institutions in 2 countries.

Aisha FarhanaDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, USA.
Vikram Saini
Ashwani Kumar
Jack R Lancaster
Adrie J C Steyn
University of Alabama at Birmingham · USInstitute of Microbial Technology · IN

Funding

WhiB3 in M. tuberculosis virulenceR01AI058131 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI STEYN, ADRIE JC · 2004 to 2014
$3.6M
Biological Chemistry of Reactive Nitrogen Species Signaling in Cancer EtiologyR01CA131653 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI LANCASTER, JACK R · 2009 to 2013
$1.5M
MECHANISM OF MYCOBACTERIUM TUBERCULOSIS PERSISTENCER01AI076389 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI STEYN, ADRIE JC · 2009 to 2012
$1.4M
Role of WhiB3 in M. tuberculosis virulenceR56AI058131 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI STEYN, ADRIE JC · 2009 to 2009
$366k
NCI NIH HHS CA131653NIAID NIH HHS AI058131NIAID NIH HHS AI076389NIAID NIH HHS R01 AI076389
6 · The paper itself

Abstract

significanceHeme is an important prosthetic group required in a wide array of functions, including respiration, photosynthesis, metabolism, O(2) transport, xenobiotic detoxification, and peroxide production and destruction, and is an essential cofactor in proteins such as catalases, peroxidases, and members of the cytochrome P450 superfamily. Importantly, bacterial heme-based sensor proteins exploit the redox chemistry of heme to sense environmental gases and the intracellular redox state of the cell. RECENT ADVANCES: The bacterial proteins FixL (Rhizobium ssp.), CooA (Rhodospirillum rubrum), EcDos (Escherichia. coli), RcoM (Burkholderia xenovorans), and particularly Mycobacterium tuberculosis (Mtb) DosS and DosT have emerged as model paradigms of environmental heme-based sensors capable of detecting multiple gases including NO, CO, and O(2). CRITICAL ISSUES: How the diatomic gases NO, CO, or O(2) bind to heme iron to generate Fe-NO, Fe-CO, and Fe-O(2) bonds, respectively, and how the oxidation of heme iron by O(2) serves as a sensing mechanism that controls the activity of key proteins is complex and largely unclear. This is particularly important as many bacterial pathogens, including Mtb, encounters three overlapping host gases (NO, CO, and O(2)) during human infection. FUTURE DIRECTIONS: Heme is an important prosthetic group that monitors the microbe's internal and external surroundings to alter signal transduction or enzymatic activation. Modern expression, metabolomic and biochemical technologies combined with in vivo pathogenesis studies should provide fresh insights into the mechanism of action of heme-based redox sensors.

Indexed as

Bacterial ProteinsHemeHeme-Binding ProteinsHemeproteinsSignal TransductionBacterial ProteinsHemeHeme-Binding Proteinsheme protein, bacteriaHemeproteins

Identifiers

PMID22494151
PMCPMC3430476
OpenAlexW2032269392

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.