ReviewJournal of inorganic biochemistry2014
Hydrogen sulfide activation in hemeproteins: the sulfheme scenario.
Review in Journal of inorganic biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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.
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.
Who cites it
34 citing papers in PubMed, 90 citations in OpenAlex.
- Lactoperoxidase catalytically oxidize hydrogen sulfide via intermediate formation of sulfheme derivatives.Redox biochemistry and chemistry · 2024Article
- Chemistry of Hydrogen Sulfide-Pathological and Physiological Functions in Mammalian Cells.Cells · 2023Review
- Low level exposure to hydrogen sulfide: a review of emissions, community exposure, health effects, and exposure guidelines.Critical reviews in toxicology · 2023Review
- Interactions of reactive sulfur species with metalloproteins.Redox biology · 2023Review
- Review
- Cysteine Biosynthesis inBiomolecules · 2022Article
- Recent Development of the Molecular and Cellular Mechanisms of Hydrogen Sulfide Gasotransmitter.Antioxidants (Basel, Switzerland) · 2022Review
- The Pathophysiology of HBiomolecules · 2022Review
- Fluoride binding to characteristic heme-pocket centers: Insights into ligand stability.Journal of inorganic biochemistry · 2021Article
- HBiomedicines · 2021Review
- New possible silver lining for pancreatic cancer therapy: Hydrogen sulfide and its donors.Acta pharmaceutica Sinica. B · 2021Review
- Understanding hydrogen sulfide signaling in neonatal airway disease.Expert review of respiratory medicine · 2021Review
- Hydrogen Sulfide: From a Toxic Molecule to a Key Molecule of Cell Life.Antioxidants (Basel, Switzerland) · 2020Review
- Hydrogen Sulfide in Pharmacotherapy, Beyond the Hydrogen Sulfide-Donors.Biomolecules · 2020Review
- Hydrogen Sulfide Metabolism and Signaling in the Tumor Microenvironment.Advances in experimental medicine and biology · 2020Review
- A reaction pathway to compound 0 intermediates in oxy-myoglobin through interactions with hydrogen sulfide and His64.Journal of molecular graphics & modelling · 2020Article
- Hydrogen sulfide signaling in mitochondria and disease.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Review
- Role of Gender in Regulation of Redox Homeostasis in Pulmonary Arterial Hypertension.Antioxidants (Basel, Switzerland) · 2019Review
- Hydrogen Sulfide and Persulfides Oxidation by Biologically Relevant Oxidizing Species.Antioxidants (Basel, Switzerland) · 2019Review
- Characterization of Recombinant His-Tag Protein Immobilized onto Functionalized Gold Nanoparticles.Sensors (Basel, Switzerland) · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Traditionally known as a toxic gas, hydrogen sulfide (H2S) is now recognized as an important biological molecule involved in numerous physiological functions. Like nitric oxide (NO) and carbon monoxide (CO), H2S is produced endogenously in tissues and cells and can modulate biological processes by acting on target proteins. For example, interaction of H2S with the oxygenated form of human hemoglobin and myoglobin produces a sulfheme protein complex that has been implicated in H2S degradation. The presence of this sulfheme derivative has also been used as a marker for endogenous H2S synthesis and metabolism. Remarkably, human catalases and peroxidases also generate this sulfheme product. In this review, we describe the structural and functional aspects of the sulfheme derivative in these proteins and postulate a generalized mechanism for sulfheme protein formation. We also evaluate the possible physiological function of this complex and highlight the issues that remain to be assessed to determine the role of sulfheme proteins in H2S metabolism, detection and physiology.
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Registered trials
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.