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Related Concept Videos

Preparation and Reactions of Thiols02:33

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.
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Redox Reactions01:24

Redox Reactions

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Oxidation-reduction or redox reactions involve the transfer of electrons from one molecule or atom to another. When an atom gains an electron, another atom must lose an electron, meaning oxidation and reduction must occur together. Since the redox occurs in pairs, the atom that gets oxidized is also called the reducing agent or reductant, and the atom that is reduced is also called the oxidizing agent or oxidant. A straightforward way to remember the definitions of oxidation and reduction is...
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Redox Reactions01:27

Redox Reactions

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Redox reactions are vital biochemical processes that underpin energy metabolism in cells. These reactions involve the transfer of electrons between molecules, occurring in tandem as oxidation and reduction. Oxidation refers to the loss of electrons, while reduction denotes their gain. This coupling ensures the seamless flow of electrons through metabolic pathways. For example, in bacterial metabolism, glucose undergoes oxidation to carbon dioxide, while oxygen is simultaneously reduced to...
1.4K
Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

5.4K
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.
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox...
5.4K
Protein Modifications in the RER01:26

Protein Modifications in the RER

7.7K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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...
7.7K
Redox Titration: Other Oxidizing and Reducing Agents01:26

Redox Titration: Other Oxidizing and Reducing Agents

1.8K
Besides iodine, other oxidizing or reducing agents can serve as titrants in redox titrations. Common oxidizing titrants include KMnO4, cerium(IV), and K2Cr2O7. The choice of oxidizing titrants depends on factors like stability, cost, analyte strength, and reaction rate between the analyte and titrant. KMnO4 is a strong oxidizing titrant that reduces from Mn(VII) to Mn(II) in a highly acidic solution, simultaneously oxidizing the analyte to a higher oxidation state. In this case, KMnO4 acts as a...
1.8K

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Related Experiment Video

Updated: Apr 16, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
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Thiol-based redox switches in prokaryotes.

Melanie Hillion, Haike Antelmann

    Biological Chemistry
    |February 27, 2015
    PubMed
    Summary

    Bacteria use thiol-based redox sensors to detect harmful reactive oxygen species (ROS), reactive electrophilic species (RES), and hypochlorous acid (HOCl), regulating detoxification and virulence in pathogens.

    Area of Science:

    • Microbiology
    • Molecular Biology
    • Biochemistry

    Background:

    • Bacteria face oxidative stress from aerobic respiration and host immune responses, encountering reactive oxygen species (ROS), reactive electrophilic species (RES), and hypochlorous acid (HOCl).
    • These reactive molecules target cysteine thiol groups in proteins, triggering thiol-disulfide switches in redox-sensing regulators to maintain cellular redox balance and activate defense mechanisms.

    Purpose of the Study:

    • To review bacterial thiol-based redox sensors that detect ROS, RES, and HOCl through thiol-dependent mechanisms.
    • To highlight the role of these sensors in regulating gene transcription in Gram-positive bacteria, including human pathogens like Staphylococcus aureus and Mycobacterium tuberculosis.
    • To focus on newly identified HOCl-specific redox regulators in Escherichia coli.

    Main Methods:

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    Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
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    Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
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    Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
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    • Review of existing literature on bacterial thiol-based redox sensing mechanisms.
    • Analysis of diverse sensing strategies including thiol-disulfide switches, cysteine phosphorylation, thiol-S-alkylation, and methionine oxidation.
    • Examination of specific redox regulators such as OxyR, OhrR, HypR, YodB, NemR, RclR, Spx, RsrA/RshA, SarZ, MgrA, SarA, QsrR, PerR, and HypT.

    Main Results:

    • Identified various 1-Cys-type and 2-Cys-type thiol-based redox sensors employing distinct mechanisms to respond to ROS, RES, and HOCl.
    • Demonstrated that these sensors regulate gene transcription, crucial for detoxification pathways and adaptation to host environments.
    • Highlighted the significance of these regulators in virulence and host immune defense adaptation in pathogenic bacteria.

    Conclusions:

    • Bacterial thiol-based redox sensors are essential for sensing and responding to diverse oxidative and electrophilic stresses.
    • These regulators play a critical role in bacterial survival, adaptation, and virulence, particularly in pathogenic species.
    • Emerging research continues to uncover novel redox-sensing mechanisms and their implications in bacterial pathogenesis.