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Related Concept Videos

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.
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.
Electrophilic Aromatic Substitution: Sulfonation of Benzene01:22

Electrophilic Aromatic Substitution: Sulfonation of Benzene

Sulfonation of benzene is a reaction wherein benzene is treated with fuming sulfuric acid at room temperature to produce benzenesulfonic acid. Fuming sulfuric acid is a mixture of sulfur trioxide and concentrated sulfuric acid.

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Related Experiment Video

Updated: May 30, 2026

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

Multiple ways to make disulfides.

Neil J Bulleid1, Lars Ellgaard

  • 1Institute of Molecular, Cellular and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK. neil.bulleid@glasgow.ac.uk

Trends in Biochemical Sciences
|July 23, 2011
PubMed
Summary
This summary is machine-generated.

Disulfide bond formation in the endoplasmic reticulum (ER) involves more than just ERO1. Alternative pathways and glutathione play key roles in this essential protein modification process.

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Synthesis of a Thiol Building Block for the Crystallization of a Semiconducting Gyroidal Metal-sulfur Framework
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Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
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Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

Related Experiment Videos

Last Updated: May 30, 2026

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

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Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • The formation of disulfide bonds is crucial for protein folding and function within the secretory pathway.
  • Endoplasmic reticulum (ER) oxidoreductin 1 (ERO1) was initially considered the primary enzyme for de novo disulfide bond formation.
  • Mammalian survival and disulfide bond formation in the absence of ERO1 indicate the existence of alternative pathways.

Purpose of the Study:

  • To review and discuss the various pathways involved in disulfide bond formation in the mammalian ER.
  • To highlight the regulatory role of glutathione in disulfide bond formation.
  • To update the understanding of disulfide bond formation beyond the ERO1 pathway.

Main Methods:

  • Literature review of recent findings on disulfide bond formation pathways.
  • Discussion of enzymes such as peroxiredoxin 4, quiescin sulfhydryl oxidase, ER-localized protein disulfide isomerase peroxidases, and vitamin K epoxide reductase.
  • Analysis of the role of glutathione in regulating oxidative protein folding.

Main Results:

  • ERO1 is not the sole contributor to disulfide bond formation in the ER.
  • Peroxiredoxin 4 is implicated in peroxide removal and disulfide formation.
  • Multiple less-characterized pathways contribute to disulfide formation, with glutathione acting as a central regulator.

Conclusions:

  • Disulfide bond formation in the mammalian ER is a complex process involving multiple enzymatic pathways.
  • Alternative pathways to ERO1 are essential for disulfide bond formation.
  • Glutathione plays a critical regulatory role in oxidative protein folding within the ER.