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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.
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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.
Phase II Reactions: Methylation Reactions01:17

Phase II Reactions: Methylation Reactions

Methylation is a phase II biotransformation process involving the attachment of a methyl group to a substrate. Enzymes known as methyltransferases orchestrate this reaction.
The mechanism of methylation unfolds in two stages. The first stage sees a methyltransferase enzyme facilitating the transfer of a methyl group from S-adenosylmethionine (SAM) to the substrate, forming S-adenosylhomocysteine (SAH). The second stage involves further metabolism of SAH into homocysteine, which can be recycled...
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Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation

Glutathione, a tripeptide made up of glutamate, cysteine, and glycine, is a critical player in the detoxification of drugs and xenobiotics via a process known as glutathione conjugation or mercapturic acid formation. This phase II biotransformation reaction involves the covalent binding of glutathione to a drug or its metabolite, enhancing the compound's water solubility and enabling its excretion.
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Aldehydes and Ketones to Alkenes: Wittig Reaction Overview01:19

Aldehydes and Ketones to Alkenes: Wittig Reaction Overview

The Wittig reaction is the conversion of carbonyl compounds-aldehydes and ketones-to alkenes using phosphorus ylides, or the Wittig reagent. The reaction was pioneered by Prof. Georg Wittig, for which he was awarded the Nobel Prize in Chemistry.
Multiple Halogenation of Methyl Ketones: Haloform Reaction01:28

Multiple Halogenation of Methyl Ketones: Haloform Reaction

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Related Experiment Video

Updated: Jul 6, 2026

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

New light on methylthiolation reactions.

M Fontecave1, E Mulliez, M Atta

  • 1Laboratoire de Chimie et Biologie des Métaux, UMR 5249, Université Joseph Fourier, CEA, CNRS, 17 Avenue des Martyrs, 38054 Grenoble Cedex 9, France. M.Fontecave.mfontecave@cea.fr

Chemistry & Biology
|March 22, 2008
PubMed
Summary

A novel enzyme, RimO, methylthiolates a specific aspartate on ribosomal protein S12 in E. coli. This ribosomal modification enzyme is similar to MiaB, which modifies tRNAs.

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Last Updated: Jul 6, 2026

Synthesis of a Thiol Building Block for the Crystallization of a Semiconducting Gyroidal Metal-sulfur Framework
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Published on: April 9, 2018

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Ribosomal proteins are crucial for ribosome function.
  • Post-translational modifications can impact protein function.
  • Methylthiolation is a key modification in biological systems.

Purpose of the Study:

  • To characterize a novel enzyme involved in ribosomal modification.
  • To elucidate the function of the RimO enzyme.
  • To compare RimO with other known methylthiolation enzymes.

Main Methods:

  • Enzyme assays to determine catalytic activity.
  • Site-directed mutagenesis to identify key residues.
  • Comparison of enzyme sequences and structures.

Main Results:

  • Identified and characterized a novel enzyme, RimO.
  • RimO catalyzes the methylthiolation of aspartate 88 on the S12 ribosomal protein.
  • Demonstrated strong similarity between RimO and the iron-sulfur enzyme MiaB.

Conclusions:

  • RimO is a novel enzyme responsible for a specific ribosomal protein modification.
  • The findings expand the understanding of post-translational modifications in ribosomes.
  • RimO represents a new class of methylthiolation enzymes with potential implications for tRNA modification research.