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

Sulfur Assimilation01:20

Sulfur Assimilation

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 become...
Preparation and Reactions of Sulfides02:26

Preparation and Reactions of Sulfides

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.
Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

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.
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Microbes and the Sulfur Cycle01:29

Microbes and the Sulfur Cycle

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 cycle.In oxic environments,...
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...

You might also read

Related Articles

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

Sort by
Same author

Genetic Analysis, Transcriptome Analysis, and Candidate Major Genes Screening of Peduncle Length Trait in Brewing Sorghum [<i>Sorghum bicolor</i> (L.) Moench].

Genes·2026
Same author

Geometry-Programmable Light-Driven Silicon Microrobots.

Advanced materials (Deerfield Beach, Fla.)·2026
Same author

NFS1 Regulates IDH2 to Attenuate Abdominal Aortic Aneurysms via Interacting With SP2.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same author

Crosstalk Between H<sub>2</sub>S and Hormones: The Bilateral Relationship and Molecular Mechanisms.

Handbook of experimental pharmacology·2025
Same author

Brassinin Induces H<sub>2</sub>S Signals and Improves Vascular Smooth Muscle Cell Functions.

Molecules (Basel, Switzerland)·2025
Same author

Localized delivery and retention of hydrogen sulfide causing regional lipid accumulation in mouse adipose tissues in vivo.

Communications biology·2025

Related Experiment Video

Updated: Jun 18, 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

H2S signals through protein S-sulfhydration.

Asif K Mustafa1, Moataz M Gadalla, Nilkantha Sen

  • 1Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

Science Signaling
|November 12, 2009
PubMed
Summary

Hydrogen sulfide (H2S) modifies proteins via S-sulfhydration, a newly identified physiologic posttranslational modification. This process impacts key proteins like GAPDH and actin, revealing H2S signaling mechanisms.

More Related Videos

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
11:33

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

Related Experiment Videos

Last Updated: Jun 18, 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

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
11:33

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Physiology

Background:

  • Hydrogen sulfide (H2S) is a known physiological vasorelaxant.
  • The precise signaling mechanisms of H2S have remained largely unknown.

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying H2S physiological signaling.
  • To identify the posttranslational modifications mediated by H2S.

Main Methods:

  • Investigated protein S-sulfhydration using biochemical assays.
  • Analyzed the impact of sulfhydration on protein function in liver cells.

Main Results:

  • Demonstrated that H2S physiologically modifies protein cysteines through S-sulfhydration.
  • Found that 10-25% of liver proteins, including actin, tubulin, and GAPDH, are sulfhydrated under normal conditions.
  • Showed that sulfhydration enhances GAPDH activity and actin polymerization.

Conclusions:

  • S-sulfhydration is a significant physiological posttranslational modification.
  • H2S signaling involves the S-sulfhydration of numerous proteins, impacting their function.
  • This discovery provides a new understanding of H2S's role in cellular processes.