Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Microbes and the Sulfur Cycle01:29

Microbes and the Sulfur Cycle

1
Sulfur is a vital element in Earth's biogeochemical systems. It transitions through various inorganic states, including sulfate (SO₄²⁻), elemental sulfur (S⁰), and sulfide (S²⁻). Abiotic and biological mechanisms across oxic and anoxic environments intricately mediate these transformations. Sulfate, the most oxidized form of sulfur, is predominantly stored in rocks, marine sediments, and oceanic waters, acting as a long-term reservoir in the global sulfur...
1
Sulfur Assimilation01:20

Sulfur Assimilation

477
Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to...
477
Anoxygenic Photosynthesis01:30

Anoxygenic Photosynthesis

1.6K
Anoxygenic photosynthesis is a phototrophic process that captures light energy to drive carbon fixation without producing molecular oxygen. Unlike oxygenic photosynthesis, which utilizes water as an electron donor and releases oxygen, anoxygenic phototrophs use alternative electron donors such as hydrogen sulfide (H₂S), elemental sulfur (S⁰), or thiosulfate (S₂O₃²⁻). This process is carried out by diverse groups of bacteria, including purple bacteria, green...
1.6K
Preparation and Reactions of Sulfides02:26

Preparation and Reactions of Sulfides

5.9K
Sulfides are the sulfur analog of ethers, just as thiols are the sulfur analog of alcohol. Like ethers, sulfides also consist of two hydrocarbon groups bonded to the central sulfur atom. Depending upon the type of groups present, sulfides can be symmetrical or asymmetrical. Symmetrical sulfides can be prepared via an SN2 reaction between 2 equivalents of an alkyl halide and one equivalent of sodium sulfide.
5.9K
Acid Mine Drainage01:19

Acid Mine Drainage

11
Mining activities that disturb sulfide-rich rocks, particularly those containing pyrite (FeS₂), initiate a cascade of geochemical and microbiological processes with serious environmental implications. When exposed to air and water, pyrite undergoes oxidation, releasing sulfate, ultimately forming sulfuric acid and mobilizing heavy metals into surrounding water systems. This phenomenon, known as acid mine drainage (AMD), results in low pH waters laden with toxic elements that threaten...
11
Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

7.9K
Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol.
7.9K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Choline-dependent methionine metabolism supports leukemia progression.

Communications biology·2026
Same author

Genomic characterization of multidrug-resistant Klebsiella pneumoniae clinical isolates from India.

Scientific reports·2026
Same author

Sulfide dynamics at the gut-microbiota interface: diet, oxygen and redox interplay.

Gut microbes·2026
Same author

The Role of Iron-Hyponitrite Intermediates in Biology and Insights From Synthetic Model Complexes.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026
Same author

Iron-addicted colorectal cancers exploit heme-complex II axis to resist oxidative cell death.

Cell metabolism·2026
Same author

Alanine Rewires the Communication Pathways Established During the Allosteric Activation of Liver Pyruvate Kinase by Fructose Bisphosphate.

Journal of chemical information and modeling·2026

Related Experiment Video

Updated: Mar 19, 2026

A Sensitive Visual Method for the Detection of Hydrogen Sulfide Producing Bacteria
03:55

A Sensitive Visual Method for the Detection of Hydrogen Sulfide Producing Bacteria

Published on: June 27, 2022

4.4K

Hydrogen Sulfide Oxidation by Myoglobin.

Trever Bostelaar, Victor Vitvitsky, Jacques Kumutima

  • 1Department of Pharmaceutical Science, Wayne State University , Detroit, Michigan 48201-2417, United States.

Journal of the American Chemical Society
|June 17, 2016
PubMed
Summary
This summary is machine-generated.

Myoglobin, like hemoglobin, can oxidize toxic hydrogen sulfide (H2S) into less harmful substances. This finding may explain why skeletal muscles are vulnerable to H2S poisoning in certain metabolic disorders.

More Related Videos

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.8K
Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
08:57

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Published on: February 24, 2018

10.6K

Related Experiment Videos

Last Updated: Mar 19, 2026

A Sensitive Visual Method for the Detection of Hydrogen Sulfide Producing Bacteria
03:55

A Sensitive Visual Method for the Detection of Hydrogen Sulfide Producing Bacteria

Published on: June 27, 2022

4.4K
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.8K
Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
08:57

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Published on: February 24, 2018

10.6K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Toxicology

Background:

  • Hydrogen sulfide (H2S) is a signaling molecule produced from amino acids, but toxic at high concentrations.
  • Cells possess mechanisms to detoxify H2S, primarily through mitochondrial sulfide oxidation.
  • Ferric hemoglobin was previously found to oxidize H2S, suggesting other heme proteins might share this function.

Purpose of the Study:

  • To investigate the capacity of myoglobin to oxidize hydrogen sulfide (H2S).
  • To characterize the iron-bound sulfur intermediates formed during H2S oxidation by myoglobin.
  • To explore the potential role of myoglobin in H2S detoxification and its relevance to specific diseases.

Main Methods:

  • Cryo-mass spectrometry and X-ray absorption spectroscopy were used to trap and analyze sulfur intermediates.
  • Electron Paramagnetic Resonance (EPR) and resonance Raman spectroscopy provided further evidence for reaction intermediates.
  • Density functional theory (DFT) calculations were employed to support mechanistic hypotheses.

Main Results:

  • Myoglobin was confirmed to oxidize hydrogen sulfide (H2S) to thiosulfate and other sulfur products.
  • Iron-bound sulfur intermediates, including hydropolysulfides, were successfully trapped and characterized.
  • Spectroscopic and computational data provided strong support for the proposed oxidation pathway.

Conclusions:

  • Myoglobin plays a significant role in the oxidation of hydrogen sulfide (H2S), similar to hemoglobin.
  • The characterization of sulfur intermediates elucidates the mechanism of H2S detoxification by myoglobin.
  • Myoglobin may concentrate H2S in skeletal muscle, potentially explaining its sensitivity to sulfide poisoning in ethylmalonic encephalopathy.