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

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.
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.
Structure and Nomenclature of Thiols and Sulfides02:17

Structure and Nomenclature of Thiols and Sulfides

Thiols and sulfides are sulfur analogs of alcohols and ethers, respectively, where the sulfur atom takes the place of the oxygen atom. Thus, thiols are generally represented as RSH, where R is an alkyl substituent and —SH is the functional group. On the other hand, in sulfides, the central sulfur atom is bonded to two hydrocarbon groups on either side. Depending upon the type of group, sulfides can be either symmetrical or asymmetrical. Both thiols and sulfides display a bent geometry, similar...
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...
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,...

You might also read

Related Articles

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

Sort by
Same author

The co-localizing Zorya II, Druantia III, and ARMADA II defense systems on O-island 172 confer synergistic anti-phage defense in enterohemorrhagic <i>Escherichia coli</i>.

mBio·2026
Same author

Beyond <i>difficile</i>: three novel toxin B-producing <i>Clostridioides</i> species from human patients with diarrhea.

Emerging microbes & infections·2026
Same author

Community context reshapes microbial proteomes and reduces functional overlap.

Nature microbiology·2026
Same author

The outer membrane vesicle-associated peptidyl-arginine deiminase of Porphyromonas gingivalis is required for macrophage evasion and modulates blood-brain barrier passage in vitro.

Microbiological research·2026
Same author

Fructan utilization by members of marine Gammaproteobacteria involves SusC/D-like proteins.

The ISME journal·2026
Same author

Impact of SliP4 deletion on the high-light acclimation in <i>Synechocystis</i> sp. PCC 6803.

microLife·2026

Related Experiment Video

Updated: May 11, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

Polysulfides link H2S to protein thiol oxidation.

Romy Greiner1, Zoltán Pálinkás, Katrin Bäsell

  • 11 Division of Redox Regulation, German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance , Heidelberg, Germany .

Antioxidants & Redox Signaling
|May 8, 2013
PubMed
Summary

Polysulfides, not hydrogen sulfide (H2S), are the oxidizing agents responsible for protein thiol modifications. This study reveals that sulfane sulfur, carried by polysulfides, is the key in vivo signaling molecule.

More Related Videos

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

Synthesis of a Thiol Building Block for the Crystallization of a Semiconducting Gyroidal Metal-sulfur Framework
12:30

Synthesis of a Thiol Building Block for the Crystallization of a Semiconducting Gyroidal Metal-sulfur Framework

Published on: April 9, 2018

Related Experiment Videos

Last Updated: May 11, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

Synthesis of a Thiol Building Block for the Crystallization of a Semiconducting Gyroidal Metal-sulfur Framework
12:30

Synthesis of a Thiol Building Block for the Crystallization of a Semiconducting Gyroidal Metal-sulfur Framework

Published on: April 9, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Hydrogen sulfide (H2S) is recognized as a gaseous signaling molecule involved in various physiological processes.
  • Its proposed mechanism of action includes protein S-sulfhydration, modifying cysteinyl thiolates to persulfides.
  • A key unresolved question is how H2S, with sulfur in its lowest oxidation state, causes oxidative thiol modifications.

Purpose of the Study:

  • To elucidate the mechanism by which hydrogen sulfide (H2S) induces oxidative thiol modifications in proteins.
  • To identify the specific species responsible for these oxidative changes.
  • To clarify the role of H2S in cellular signaling pathways.

Main Methods:

  • Utilized the lipid phosphatase PTEN as a model protein to study H2S-induced oxidation in vitro.
  • Employed various H2S donors, including sodium hydrosulfide (NaHS), sodium sulfide (Na2S), gaseous H2S, and GYY4137.
  • Investigated the modification of PTEN within intact cells exposed to H2S solutions.

Main Results:

  • Sodium hydrosulfide (NaHS) rapidly and reversibly oxidized PTEN in vitro.
  • Identified polysulfides in H2S solutions as the active oxidizing species, adding sulfane sulfur to the active site cysteine.
  • Demonstrated that polysulfides mediate PTEN oxidation induced by all tested H2S donors, both in vitro and in intact cells.

Conclusions:

  • Polysulfides, formed in H2S solutions, are the mediators of protein thiol oxidation previously attributed to H2S.
  • These findings resolve the question of how H2S, a reducing agent, can cause oxidative modifications.
  • The study supports the conclusion that sulfane sulfur, rather than sulfide, is the primary in vivo signaling agent of H2S.