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Related Concept Videos

Preparation and Reactions of Sulfides02:26

Preparation and Reactions of Sulfides

6.0K
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.
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Sulfur Assimilation01:20

Sulfur Assimilation

494
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...
494
Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

7.9K
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.
7.9K
Preparation of Amines: Reduction of Oximes and Nitro Compounds01:29

Preparation of Amines: Reduction of Oximes and Nitro Compounds

4.9K
Oximes can be reduced to primary amines using catalytic hydrogenation, hydride reduction, or sodium metal reduction. The reduction of aliphatic and aromatic nitro compounds to primary amines takes place by either catalytic hydrogenation or by using active metals like Fe, Zn, and Sn in the presence of an acid.
Though catalytic hydrogenation can reduce nitrobenzenes, the reduction is nonselective in the presence of other functional groups. For instance, if nitrobenzene contains an aldehyde group,...
4.9K
Oxidation and Reduction of Organic Molecules01:19

Oxidation and Reduction of Organic Molecules

10.6K
Energy production within a cell involves many coordinated chemical pathways. Most of these pathways are combinations of oxidation and reduction reactions, which occur at the same time. An oxidation reaction strips an electron from an atom in a compound, and the addition of this electron to another compound is a reduction reaction. Because oxidation and reduction usually occur together, these pairs of reactions are called redox reactions.
The removal of an electron from a molecule, results in a...
10.6K
Oxymercuration-Reduction of Alkenes02:36

Oxymercuration-Reduction of Alkenes

9.8K
Oxymercuration–reduction of alkenes is one of the major reactions converting alkenes to alcohols. It involves the hydration of alkenes with mercuric acetate in a mixture of tetrahydrofuran and water, forming an organomercury adduct. This is followed by a demercuration step in which the adduct is reduced to an alcohol using sodium borohydride.
9.8K

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Related Experiment Video

Updated: Apr 1, 2026

Measuring Trans-Plasma Membrane Electron Transport by C2C12 Myotubes
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Selenium and Methionine Sulfoxide Reduction.

Vadim N Gladyshev1

  • 1Brigham and Women׳s Hospital, Harvard Medical School, Boston, USA.

Free Radical Biology & Medicine
|October 14, 2015
PubMed
Summary

Selenium-dependent MsrB1 regulates actin dynamics by reversing methionine oxidation. This redox control is crucial for macrophage activation and cellular function, revealing a new layer of protein regulation.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Selenium is an essential trace element incorporated into selenoproteins.
  • Selenoproteins, such as methionine-R-sulfoxide reductase B1 (MsrB1), are primarily oxidoreductases.
  • MsrB1 functions as a repair enzyme, reducing oxidized methionine residues in proteins.

Purpose of the Study:

  • To investigate if reversible methionine oxidation regulates protein function.
  • To elucidate the role of MsrB1 and Mical proteins in actin dynamics.
  • To understand the mechanism of redox control in macrophage activation.

Main Methods:

  • Investigated the interaction between MsrB1, Mical proteins, and actin.
  • Analyzed the stereospecific oxidation and reduction of methionine residues in actin.

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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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  • Examined the effect of MsrB1 expression and activity on macrophage cellular activation.

    • Main Results:

    • MsrB1 and Mical proteins reversibly regulate mammalian actin assembly through site-specific methionine oxidation and reduction.
    • Mical1 and Mical2 oxidize specific actin methionine residues to methionine-R-sulfoxide.
    • MsrB1 reduces these oxidized residues, facilitating actin disassembly and assembly.
    • Macrophages use this redox control during activation, upregulating MsrB1.

    Conclusions:

    • MsrB1 acts as a Mical antagonist, orchestrating actin dynamics and macrophage function.
    • Protein function can be regulated by reversible, site-specific methionine-R-sulfoxidation.
    • Selenium, via MsrB1, plays a critical role in this regulatory mechanism.