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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.

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The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
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During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...

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Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

Published on: March 24, 2012

How thioredoxin dissociates its mixed disulfide.

Goedele Roos¹, Nicolas Foloppe, Koen Van Laer

¹Department of Molecular and Cellular Interactions, Vlaams Interuniversitair Instituut voor Biotechnologie, Brussels, Belgium. groos@vub.ac.be

Plos Computational Biology

|August 14, 2009

Summary

This summary is machine-generated.

The thioredoxin (Trx) mixed disulfide dissociation mechanism was clarified. A key cysteine residue (Cys32) on Trx is activated to attack the intermediate disulfide, resolving a long-standing debate on thiol/disulfide exchange reactions.

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

The dissociation mechanism of thioredoxin (Trx) mixed disulfide complexes remains debated for over two decades.
Opposing views exist regarding the activation of nucleophilic cysteine residues as thiolates during complex dissociation.

Purpose of the Study:

To elucidate the dissociation mechanism of Trx mixed disulfide complexes using the Trx-arsenate reductase (ArsC) model.
To investigate the role of specific cysteine residues in the thiol/disulfide exchange reaction.

Main Methods:

Theoretical reactivity analysis
Molecular dynamics simulations
Biochemical experiments with cysteine mutants

Main Results:

Conformational changes position Cys32(Trx) for nucleophilic attack on the Cys29(Trx)-Cys89(ArsC) intermediate disulfide.
Cys32(Trx) activation via hydrogen bonding enhances its reactivity compared to Cys82(ArsC).
Cys32(Trx) preferentially attacks Cys29(Trx), not Cys89(ArsC), leading to substrate reduction and Trx oxidation.

Conclusions:

The study provides a detailed, multidisciplinary understanding of Trx mixed disulfide complex dissociation.
Findings resolve the debate on cysteine thiolate activation in thiol/disulfide exchange reactions.
The mechanism elucidated is applicable to universal thiol/disulfide exchange processes.