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Related Concept Videos

Oxidation of Alcohols02:37

Oxidation of Alcohols

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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:
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Protein Modifications in the RER01:26

Protein Modifications in the RER

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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.
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Radical Autoxidation01:20

Radical Autoxidation

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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...
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Radical Reactivity: Steric Effects01:10

Radical Reactivity: Steric Effects

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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...
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Oxidation of Alkenes: Anti Dihydroxylation with Peroxy Acids02:04

Oxidation of Alkenes: Anti Dihydroxylation with Peroxy Acids

7.0K
Diols are compounds with two hydroxyl groups. In addition to syn dihydroxylation, diols can also be synthesized through the process of anti dihydroxylation. The process involves treating an alkene with a peroxycarboxylic acid to form an epoxide. Epoxides are highly strained three-membered rings with oxygen and two carbons occupying the corners of an equilateral triangle. This step is followed by ring-opening of the epoxide in the presence of an aqueous acid to give a trans diol.
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Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

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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.
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Updated: Dec 8, 2025

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

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Implication of Staphylococcus aureus MsrB dimerization upon oxidation.

Hyo Jung Kim1

  • 1College of Pharmacy, Woosuk University, Wanju, 55338, Republic of Korea.

Biochemical and Biophysical Research Communications
|September 18, 2020
PubMed
Summary
This summary is machine-generated.

Oxidative stress impacts bacterial virulence. This study reveals how Staphylococcus aureus Methionine Sulfoxide Reductase B (MsrB) changes structure upon oxidation, forming dimers to accept substrates and aiding redox control.

Keywords:
Methionine sulfoxide reductaseMsrBOxidationPost-translational modificationRedox enzymeStaphylococcus aureusX-ray crystallography

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Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
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Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Oxidative modification of proteins is crucial in bacterial virulence and metabolism.
  • Sulfur-containing amino acids like cysteine and methionine are prone to oxidation.
  • Methionine sulfoxide reductases (Msr) enzymes reverse methionine oxidation.

Purpose of the Study:

  • To elucidate the structure of Methionine Sulfoxide Reductase B (MsrB) from Staphylococcus aureus Mu50.
  • To investigate structural changes in MsrB upon oxidation.
  • To understand the mechanism of redox control in MsrB.

Main Methods:

  • X-ray crystallography to determine protein structure.
  • Comparative structural analysis of oxidized and reduced MsrB.
  • Biochemical assays to assess substrate binding and activity.

Main Results:

  • The active site of Staphylococcus aureus MsrB features two reduced cysteines.
  • Oxidation induces a conformational change leading to MsrB dimerization.
  • The dimeric form of MsrB creates a specific structure for peptidyl substrate binding.

Conclusions:

  • Oxidation-induced dimerization of Staphylococcus aureus MsrB is a key regulatory mechanism.
  • This structural transition facilitates substrate acceptance and likely plays a role in bacterial redox homeostasis.
  • The findings provide insights into the poorly characterized redox control mechanisms in bacteria.