Evidence map›Paper›PMID 24416422›Full record

ArticlePloS one2014

Nitrite reductase activity and inhibition of H₂S biogenesis by human cystathionine ß-synthase.

Carmen Gherasim, Pramod K Yadav, Omer Kabil, Wei-Ning Niu, Ruma Banerjee

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.9field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. A Metabolic Paradigm for Hydrogen Sulfide SignalingAntioxidants & redox signaling · 2023
    Review
  5. Review
  6. Review
  7. Article
  8. The human BThe Journal of biological chemistry · 2020
    Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Chemical Biology of HChemical reviews · 2018
    Review
  15. Review
  16. Catalytic promiscuity and heme-dependent redox regulation of HCurrent opinion in chemical biology · 2017
    Review
  17. Review
  18. Article
  19. Article
  20. 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.

Carmen GherasimDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan, United States of America.
Pramod K YadavDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan, United States of America.
Omer KabilDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan, United States of America.
Wei-Ning NiuDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan, United States of America ; School of Life Science, Northwestern Polytechnical University, Xi'an, China.
Ruma BanerjeeDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan, United States of America.
University of Michigan–Ann Arbor · USMichigan United · US

Funding

Transsulfuration and HyperhomocysteinemiaR01HL058984 · NHLBI · UNIVERSITY OF NEBRASKA LINCOLN · PI BANERJEE, RUMA V · 1997 to 2020
$6.0M
NHLBI NIH HHS HL58984NHLBI NIH HHS R01 HL058984
6 · The paper itself

Abstract

Nitrite was recognized as a potent vasodilator >130 years and has more recently emerged as an endogenous signaling molecule and modulator of gene expression. Understanding the molecular mechanisms that regulate nitrite metabolism is essential for its use as a potential diagnostic marker as well as therapeutic agent for cardiovascular diseases. In this study, we have identified human cystathionine ß-synthase (CBS) as a new player in nitrite reduction with implications for the nitrite-dependent control of H₂S production. This novel activity of CBS exploits the catalytic property of its unusual heme cofactor to reduce nitrite and generate NO. Evidence for the possible physiological relevance of this reaction is provided by the formation of ferrous-nitrosyl (Fe(II)-NO) CBS in the presence of NADPH, the human diflavin methionine synthase reductase (MSR) and nitrite. Formation of Fe(II)-NO CBS via its nitrite reductase activity inhibits CBS, providing an avenue for regulating biogenesis of H₂S and cysteine, the limiting reagent for synthesis of glutathione, a major antioxidant. Our results also suggest a possible role for CBS in intracellular NO biogenesis particularly under hypoxic conditions. The participation of a regulatory heme cofactor in CBS in nitrite reduction is unexpected and expands the repertoire of proteins that can liberate NO from the intracellular nitrite pool. Our results reveal a potential molecular mechanism for cross-talk between nitrite, NO and H₂S biology.

Indexed as

Cystathionine beta-SynthaseElectron Spin Resonance SpectroscopyHemeHumansHydrogen SulfideIronModels, BiologicalNitric OxideNitrite ReductasesNitritesOxidation-ReductionPyridoxal PhosphateReducing AgentsCystathionine beta-SynthaseHemeHydrogen SulfideIronNitric OxideNitrite ReductasesNitritesPyridoxal PhosphateReducing Agents

Identifiers

PMID24416422
PMCPMC3885727
OpenAlexW1979659625

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.