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Preparation and Reactions of Thiols

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 Sulfides

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...

Preparation and Reactions of Sulfides

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.

Sulfur Assimilation

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...

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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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Quantification of thiols and disulfides.

Jakob R Winther¹, Colin Thorpe

¹Section for Biomolecular Sciences, Department of Biology, University of Copenhagen, Copenhagen Biocenter, DK-2200 Copenhagen, Denmark.

Biochimica Et Biophysica Acta

|April 10, 2013

Summary

Disulfide bond formation is crucial for protein function but challenging to measure. Current chemical methods for determining thiols and disulfides have limitations, highlighting the need for improved tools to study cellular redox homeostasis.

Keywords:

1-cyano-4-dimethylamino-pyridinium 2-mercato ethanol 4,4′-dithiodipyridine 4-(aminosulfonyl)-7-fluoro-2,1,3-benzoxadiazole 4-DPS 4-acetamido-4′-maleimidylstilbene-2,2′-disulfonic acid 5,5′-dithiobis-(2-nitrobenzoic) acid 5-thio-2-nitrobenzoic acid 7-fluorobenzo-2-oxa-1,3-diazole-4-sulfonate ABD-F AMS CDAP DTNB Detection EDTA ER Exchange GSH GSSG HMD MBBr ME MMTS Modification Monobromobimane Nucleophile PAGE PEG Redox S-methyl methanethiosulfonate SBD-F SDS TCEP THP TNB endoplasmic reticulum ethylenediamine tetraacetic acid glutathione glutathione disulfide heavy maleimide derivative polyacrylamide gel electrophoresis polyethyleneglycol sodium dodecylsulfate tris(2-carboxyethyl) phosphine tris(2-hydroxyethyl) phosphine

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Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

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Published on: March 24, 2012

Area of Science:

Biochemistry
Cellular Biology
Posttranslational Modifications

Background:

Disulfide bonds are vital posttranslational modifications affecting protein structure and function.
Cellular thiol-disulfide homeostasis is tightly regulated by multiple systems.
Measuring redox states of thiols and disulfides is complex due to facile exchange reactions.

Purpose of the Study:

To review chemical methods for determining thiols and disulfides.
To identify challenges in current thiol-disulfide measurement techniques.
To highlight the need for new tools in cellular redox research.

Main Methods:

Survey of chemical determination methods for thiols and disulfides.
Focus on key chemical aspects and experimental difficulties.
Review of reagents for thiol and disulfide redox status manipulation.

Main Results:

Numerous reagents exist for measuring and manipulating thiol-disulfide redox status.
Many described methods are underutilized in practice.
Quantifying redox changes in living cells remains a significant challenge.

Conclusions:

Effective quantification of cellular redox conditions is an ongoing challenge.
Understanding thiol-disulfide exchange pathway flux requires new tools.
Further research is needed to fully elucidate thiol and disulfide metabolism.