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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.
Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

In the presence of oxidizing agents, phenols are oxidized to quinones. Quinones can be easily reduced back to phenols using mild reducing agents. The electron-donating hydroxyl group enhances the reactivity of the aromatic ring, enabling oxidation of the ring even in the absence of an α hydrogen.
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox property is crucial in...
Radical Autoxidation01:20

Radical Autoxidation

The oxidation of an organic compound in the presence of air or oxygen is called autoxidation. For example, cumene reacts with oxygen to form hydroperoxide. Autoxidation involves initiation, propagation, and termination steps. Many organic compounds are susceptible to autoxidation—especially ethers in the presence of oxygen, which form hydroperoxides. Even though this reaction is slow, old ether bottles contain small amounts of peroxide, which leads to laboratory explosions during ether...
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.
Oxidation of Alcohols02:37

Oxidation of Alcohols

In this lesson, the oxidation of alcohols is discussed in depth. The various reagents used for oxidation of primary and secondary alcohols are detailed, and their mechanism of action is provided.
The process of oxidation in a chemical reaction is observed in any of the three forms:
Radical Reactivity: Steric Effects01:10

Radical Reactivity: Steric Effects

The presence of electron-donating, electron-withdrawing, or conjugating groups adjacent to a radical center, imparts electronic stabilization to the radicals. Examples of such electronically-stabilized radicals are triphenylmethyl, tetramethylpiperidine‐N‐oxide, and 2,2‐diphenyl‐1‐picrylhydrazyl. These radicals are remarkably stable and are known as persistent radicals. Some of the persistent radicals can even be isolated and purified.
Along with electronic factors, steric factors also account...

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Related Experiment Video

Updated: Jun 3, 2026

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

Published on: June 21, 2021

Factors affecting protein thiol reactivity and specificity in peroxide reduction.

Gerardo Ferrer-Sueta1, Bruno Manta, Horacio Botti

  • 1Laboratorio de Fisicoquímica Biológica, Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República, Montevideo, Uruguay.

Chemical Research in Toxicology
|March 12, 2011
PubMed
Summary

Peroxiredoxins exhibit remarkable thiol reactivity toward hydroperoxides by stabilizing the reaction transition state. This protein-mediated stabilization enhances catalytic efficiency and confers specificity for hydrogen peroxide sensing.

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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
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Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
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Published on: March 24, 2012

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Last Updated: Jun 3, 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
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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

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
12:07

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

Published on: March 24, 2012

Area of Science:

  • Biochemistry
  • Enzymology
  • Protein Chemistry

Background:

  • Protein thiol reactivity is crucial for various biological processes, often involving nucleophilic attack by thiolate anions.
  • While low pKa increases thiolate availability at neutral pH, it doesn't always guarantee higher nucleophilicity.
  • Peroxiredoxins display exceptionally high reaction rates in reducing hydroperoxides compared to free cysteine.

Purpose of the Study:

  • To investigate the mechanisms underlying the extraordinary catalytic efficiency and specificity of peroxiredoxin thiols.
  • To re-evaluate the role of thiolate stabilization versus transition state stabilization in peroxiredoxin catalysis.
  • To elucidate how protein structural factors confer specific thiol reactivity toward hydroperoxides.

Main Methods:

  • Analysis of electrostatic and polar interactions within the peroxiredoxin active site.
  • Characterization of the protein environment surrounding the catalytic cysteine residue.
  • Investigating the dynamic changes in protein-ligand interactions during catalysis.

Main Results:

  • Protein structure stabilizes the anionic transition state through a combination of static and dynamic interactions.
  • A conserved arginine and alpha-helix N-terminus create a cationic environment stabilizing the thiolate and transition state.
  • Dynamic polar interactions switch from stabilizing the thiolate to binding peroxide, increasing nucleophilicity and specificity.

Conclusions:

  • Catalytic efficiency in peroxiredoxins stems from transition state stabilization, not solely thiolate stabilization.
  • The enhanced acidity of the catalytic cysteine is a consequence, not the cause, of catalytic efficiency.
  • Peroxiredoxins, like glutathione peroxidases, function as essential cellular sensors for hydroperoxides due to their reactivity and specificity.