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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.

Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation

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.
Several distinctive characteristics distinguish glutathione conjugation from other phase II...

Protein Transport to the Thylakoids

Protein Transport to the Thylakoids

Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...

Electron Transport Chain: Complex III and IV

Electron Transport Chain: Complex III and IV

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...

Protein Modifications in the RER

Protein Modifications in the RER

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Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

Oxidation of Phenols to Quinones

Oxidation of Phenols to Quinones

In the presence of oxidizing agents, phenols are oxidized to quinones. Quinones can be easily reduced back to phenols using mild reducing agents. The electron-donating hydroxyl group enhances the reactivity of the aromatic ring, enabling oxidation of the ring even in the absence of an α hydrogen.
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Related Experiment Video

Updated: Jul 15, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

[Thioltransferase and thioredoxin system in cataract].

Feiyan Chai¹, Hong Yan

¹Department of Ophthalmology, Tangdu Hospital, 4th Military Medical University, Xi'an 710038, China.

Yan Ke Xue Bao = Eye Science

|April 21, 2007

Summary

Glutathione (GSH) levels decrease with age, impacting lens transparency. Thioltransferase (TTase) and thioredoxin (Trx) systems may work together to repair lens proteins and maintain eye health.

Area of Science:

Biochemistry
Ophthalmology
Cellular Redox Biology

Context:

The eye lens requires a balanced redox state for transparency.
Reduced glutathione (GSH) levels are observed in aging and cataractous lenses.
Endogenous GSH and repair enzymes are crucial for lens health.

Purpose:

To investigate the roles of thioltransferase (TTase) and thioredoxin (Trx) systems in lens redox homeostasis.
To understand how these systems may counteract GSH depletion.
To explore their synergistic potential in maintaining lens function.

Summary:

Aging and cataract lenses exhibit depleted glutathione (GSH) pools, compromising lens transparency.
Thioltransferase (TTase) specifically repairs protein-S-S-glutathione linkages, restoring free SH groups.

Related Experiment Videos

Last Updated: Jul 15, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

The thioredoxin (Trx) system repairs protein disulfides, regulating cellular redox balance.

TTase and Trx may synergistically repair lens protein thiols, preserving lens function.

Impact:

Highlights the importance of GSH and associated enzyme systems in preventing lens opacification.
Suggests TTase and Trx as potential therapeutic targets for age-related cataracts.
Provides insights into redox mechanisms underlying lens aging and disease.