Evidence map›Paper›PMID 27310035›Full record

ArticleJournal of the American Chemical Society2016

Hydrogen Sulfide Oxidation by Myoglobin.

Trever Bostelaar, Victor Vitvitsky, Jacques Kumutima, Brianne E Lewis, Pramod K Yadav, Thomas C Brunold, Milos Filipovic, Nicolai Lehnert, Timothy L Stemmler, Ruma Banerjee

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
13.2field-weighted citation impact, top 1% 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

56 citing papers in PubMed, 161 citations in OpenAlex.

  1. Article
  2. The first and second zinc finger domains from Poly-ADP-ribose polymerase 1 (PARP1) are modified by hydrogen sulfide.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Article
  3. Article
  4. Review
  5. Power and poison: The intersections of HThe Journal of biological chemistry · 2025
    Review
  6. Hydrogen sulfide/polysulfides signaling and neuronal diseases.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Emerging roles of hydrogen sulfide-metabolizing enzymes in cancer.Redox report : communications in free radical research · 2024
    Review
  12. Review
  13. Review
  14. Article
  15. HProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Article
  17. Hydrogen Sulfide (HBiomolecules · 2024
    Review
  18. Review
  19. Emerging Chemical Biology of Protein Persulfidation.Antioxidants & redox signaling · 2023
    Review
  20. 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

10 authors at 4 institutions in 2 countries.

Trever Bostelaar
Victor Vitvitsky
Jacques Kumutima
Brianne E LewisDepartment of Pharmaceutical Science, Wayne State University , Detroit, Michigan 48201-2417, United States.
Pramod K Yadav
Thomas C BrunoldDepartment of Chemistry, University of Wisconsin , Madison, Wisconsin 53706, United States.
Milos FilipovicUniversity of Bordeaux, IBGC, and CNRS, IBGC, UMR 5095 , F-33077 Bordeaux, France.
Nicolai Lehnert
Timothy L StemmlerDepartment of Pharmaceutical Science, Wayne State University , Detroit, Michigan 48201-2417, United States.
Ruma Banerjee
University of Michigan–Ann Arbor · USWayne State University · USUniversité de Bordeaux · FRUniversity of Wisconsin–Madison · US

Funding

Structural Insights into the Function of FrataxinR01DK068139 · NIDDK · WAYNE STATE UNIVERSITY · PI STEMMLER, TIMOTHY LOUIS · 2005 to 2015
$3.5M
Enzymology of Sulfide OxidationR01GM112455 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BANERJEE, RUMA V · 2014 to 2017
$1.2M
NIDDK NIH HHS R01 DK068139NIGMS NIH HHS R01 GM112455
6 · The paper itself

Abstract

Enzymes in the sulfur network generate the signaling molecule, hydrogen sulfide (H2S), from the amino acids cysteine and homocysteine. Since it is toxic at elevated concentrations, cells are equipped to clear H2S. A canonical sulfide oxidation pathway operates in mitochondria, converting H2S to thiosulfate and sulfate. We have recently discovered the ability of ferric hemoglobin to oxidize sulfide to thiosulfate and iron-bound hydropolysulfides. In this study, we report that myoglobin exhibits a similar capacity for sulfide oxidation. We have trapped and characterized iron-bound sulfur intermediates using cryo-mass spectrometry and X-ray absorption spectroscopy. Further support for the postulated intermediates in the chemically challenging conversion of H2S to thiosulfate and iron-bound catenated sulfur products is provided by EPR and resonance Raman spectroscopy in addition to density functional theory computational results. We speculate that the unusual sensitivity of skeletal muscle cytochrome c oxidase to sulfide poisoning in ethylmalonic encephalopathy, resulting from the deficiency in a mitochondrial sulfide oxidation enzyme, might be due to the concentration of H2S by myoglobin in this tissue.

Indexed as

AnimalsHorsesHydrogen SulfideIronKineticsMyoglobinOxidation-ReductionProtein BindingHydrogen SulfideIronMyoglobin

Identifiers

PMID27310035
PMCPMC5464954
OpenAlexW2442400681

What OpenQuestion holds

Textmetadata
LicenceTDM
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.