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Preparation and Reactions of Thiols

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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.

Protein Modifications in the RER

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Sulfur Assimilation

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Preparation and Reactions of Sulfides

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Phase II Reactions: Sulfation and Conjugation with α-Amino Acids

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Updated: Jun 5, 2026

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

Engineered pathways for correct disulfide bond oxidation.

Guoping Ren¹, James C A Bardwell

¹Department of Molecular, Cellular, and Developmental Biology, Howard Hughes Medical Institute, University of Michigan, 830 N. University Ave., Ann Arbor, MI 48109-1048, USA.

Antioxidants & Redox Signaling

|January 22, 2011

Summary

This summary is machine-generated.

Cells lacking protein disulfide isomerases (PDIs) can form disulfide bonds using alternative pathways. These strategies involve enhancing the DsbA oxidase or altering the periplasmic environment, mimicking eukaryotic PDI function.

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Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

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Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

Area of Science:

Biochemistry
Molecular Biology
Microbiology

Background:

Protein disulfide bond formation is essential for proper protein folding and function.
Protein disulfide isomerases (PDIs) are key enzymes facilitating correct disulfide bond formation.
Escherichia coli utilizes specific pathways, including PDIs like DsbC, for disulfide bond maturation.

Purpose of the Study:

To investigate alternative mechanisms for correct disulfide bond formation in the absence of PDIs.
To identify genetic mutations that enable disulfide bond formation without the canonical PDI DsbC.
To understand how the DsbA oxidase can acquire isomerase activity in vivo.

Main Methods:

Selection of mutants conferring antibiotic resistance linked to disulfide bond formation.
Analysis of gene expression and protein redox status in selected mutants.
Characterization of mutations affecting disulfide bond formation pathways in E. coli.

Main Results:

Mutants overproducing the disulfide oxidase DsbA and altering its redox status were identified.
Enhanced DsbA activity was observed through increased mixed disulfides with substrate proteins.
A distinct mutant mechanism involved alterations in DsbB and CpxR, impacting the periplasmic redox environment and increasing DegP levels.
This allowed DsbA to gain disulfide isomerase ability, facilitating complex disulfide bond formation.

Conclusions:

The study reveals versatile strategies for disulfide bond formation in E. coli, independent of canonical PDIs.
The oxidase DsbA can be engineered to catalyze complex disulfide bond formation with appropriate expression, redox status, and chaperone assistance.
The evolved pathways in E. coli mimic aspects of eukaryotic PDI function, highlighting conserved principles in disulfide bond management.