Evidence map›Paper›PMID 24351060›Full record

ArticleBiochemistry2013

The selectivity of Vibrio cholerae H-NOX for gaseous ligands follows the "sliding scale rule" hypothesis. Ligand interactions with both ferrous and ferric Vc H-NOX.

Gang Wu, Wen Liu, Vladimir Berka, Ah-lim Tsai

Abstract read
In one paragraph

Article in Biochemistry, 2013. 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
2.9field-weighted citation impact, top 10% 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, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Structure and reactivity of chlorite dismutase nitrosyls.Journal of inorganic biochemistry · 2020
    Article
  7. Heme inhibits the activity of a c-di-GMP phosphodiesterase in Vibrio cholerae.Biochemical and biophysical research communications · 2020
    Article
  8. Article
  9. Bacterial Heme-Based Sensors of Nitric Oxide.Antioxidants & redox signaling · 2018
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Engineering proximalChemical science · 2017
    Article
  15. Bacterial Haemoprotein Sensors of NO: H-NOX and NosP.Advances in microbial physiology · 2017
    Review
  16. Article
  17. Article
  18. Structural insights into the role of iron-histidine bond cleavage in nitric oxide-induced activation of H-NOX gas sensor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

4 authors at 2 institutions in 1 country.

Gang WuDivision of Hematology, Department of Internal Medicine, The University of Texas-Medical School at Houston , 6431 Fannin Street, Houston, Texas 77030, United States.
Wen Liu
Vladimir Berka
Ah-lim Tsai
The University of Texas at Austin · USThe University of Texas Health Science Center at Houston · US

Funding

Radical Intermediates of Nitric Oxide Synthase & Myocardial Ischemia ReperfusionR01HL095820 · NHLBI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI TSAI, AH-LIM · 2010 to 2013
$1.8M
NHLBI NIH HHS R01 HL 095820NHLBI NIH HHS R01 HL095820
6 · The paper itself

Abstract

Vc H-NOX (or VCA0720) is an H-NOX (heme-nitric oxide and oxygen binding) protein from facultative aerobic bacterium Vibrio cholerae. It shares significant sequence homology with soluble guanylyl cyclase (sGC), a NO sensor protein commonly found in animals. Similar to sGC, Vc H-NOX binds strongly to NO and CO with affinities of 0.27 nM and 0.77 μM, respectively, but weakly to O2. When positioned on a "sliding scale" plot [Tsai, A.-l., et al. (2012) Biochemistry 51, 172-186], the line connecting log K(D)(NO) and log K(D)(CO) of Vc H-NOX can almost be superimposed with that of Ns H-NOX. Therefore, the measured affinities and kinetic parameters of gaseous ligands to Vc H-NOX provide more evidence to validate the "sliding scale rule" hypothesis. Like sGC, Vc H-NOX binds NO in multiple steps, forming first a six-coordinate heme-NO complex at a rate of 1.1 × 10(9) M(-1) s(-1), and then converts to a five-coordinate heme-NO complex at a rate that is also dependent on NO concentration. Although the formation of oxyferrous Vc H-NOX cannot be detected at a normal atmospheric oxygen level, ferrous Vc H-NOX is oxidized to the ferric form at a rate of 0.06 s(-1) when mixed with O2. Ferric Vc H-NOX exists as a mixture of high- and low-spin states and is influenced by binding to different ligands. Characterization of both ferric and ferrous Vc H-NOX and their complexes with various ligands lays the foundation for understanding the possible dual roles in gas and redox sensing of Vc H-NOX.

Indexed as

Bacterial ProteinsFerric CompoundsFerrous CompoundsGuanylate CyclaseHemeKineticsLigandsNitric OxideOxygenProtein BindingReceptors, Cytoplasmic and NuclearSoluble Guanylyl CyclaseVibrio choleraeBacterial ProteinsFerric CompoundsFerrous CompoundsGuanylate CyclaseHemeLigandsNitric OxideOxygenReceptors, Cytoplasmic and NuclearSoluble Guanylyl Cyclase

Identifiers

PMID24351060
PMCPMC3999706
OpenAlexW1999484392

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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.