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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.
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 property is crucial in...

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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...

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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...

Radical Autoxidation

Radical Autoxidation

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The electron transport chain or oxidative phosphorylation is an exothermic process in which free energy released during electron transfer reactions is coupled to ATP synthesis. This process is a significant source of energy in aerobic cells, and therefore inhibitors of the electron transport chain can be detrimental to the cell's metabolic processes.
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Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q in...

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Related Experiment Video

Updated: May 9, 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 antioxidant system.

Jun Lu¹, Arne Holmgren¹

¹Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 77 Stockholm, Sweden.

Free Radical Biology & Medicine

|August 1, 2013

Summary

This summary is machine-generated.

The thioredoxin (Trx) system is crucial for antioxidant defense and cellular redox balance in both mammals and bacteria. Targeting bacterial TrxR-Trx systems offers a potential strategy against pathogens lacking other antioxidant defenses.

Keywords:

AhpC AhpF Alkyl hydroperoxide peroxidase subunit C Alkyl hydroperoxide peroxidase subunit F B. subtilis BSO Bacillus subtilis Bacterioferritin comigratory protein Bcp Buthionine sulfoximine Catalase Dihydrolipoamide succinyltransferase E. coli E. faecalis Entercoccus faecalis Escherichia coli FAD Flavin adenine dinucleotide GPx GR GSH GST Glutaredoxin Glutathione Glutathione peroxidise Glutathione reductase Glutathione transferase Grx H. pylori HDAC HTLV-1 Helicobacter pylori Histone deacetylases Human T-lymphotropic virus type I KatA KatG Keap1 Kelch-like ECH-associated protein 1 M. tuberculosis MSH Methionine-O-sulfoxide reductase Methionine-S-sulfoxide reductase Mrx MsrA MsrB Mtr Mycobacterium tuberculosis Mycoredoxin Mycothione Mycothione reductase NADPH Nicotinamide adenine dinucleotide phosphate Nrf2 Nuclear factor erythroid-related factor 2 PDI Peroxiredoxin Protein disulfide isomerase Prx RNR ROS Ribonucleotide reductase S. aureus S. pyogenes Sec Staphylococcus aureus Streptococcus pyogenes SucB TGR TS(2)TXNIP Thiol peroxidase Thioredoxin Thioredoxin glutathione reductase Thioredoxin interacting protein Thioredoxin reductase Tpx Trx TrxR TryR Trypanothione Trypanothione reductase U, selenocysteine WT Wild type antioxidant catalase peroxidase glutathione peroxiredoxin reactive oxygen species thioredoxin

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Last Updated: May 9, 2026

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

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Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

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Rapid Quantification of Oxidized and Reduced Forms of Glutathione Using Ortho -phthalaldehyde in Cultured Mammalian Cells In Vitro

Rapid Quantification of Oxidized and Reduced Forms of Glutathione Using Ortho -phthalaldehyde in Cultured Mammalian Cells In Vitro

Published on: June 28, 2024

Area of Science:

Biochemistry
Cell Biology
Microbiology

Background:

The thioredoxin (Trx) system, comprising NADPH, thioredoxin reductase (TrxR), and thiori-doxin, is a vital antioxidant defense mechanism.
It regulates protein dithiol/disulfide balance, repairs DNA and proteins, and influences immune responses and cell death.

Purpose of the Study:

To elucidate the diverse roles of the Trx system in cellular redox homeostasis.
To compare the Trx system in mammalian and bacterial cells.
To explore the potential of targeting bacterial Trx systems as an antimicrobial strategy.

Main Methods:

Review of existing literature on the thioredoxin system's structure, function, and regulation.
Comparative analysis of mammalian and bacterial Trx systems.
Identification of unique characteristics of bacterial Trx systems in specific pathogens.

Main Results:

Mammalian Trx systems, alongside the glutathione-glutaredoxin (Grx) system, maintain cellular redox balance, with cross-functionality observed.
Bacterial TrxRs differ structurally and mechanistically from mammalian counterparts.
Pathogenic bacteria like H. pylori, M. tuberculosis, and S. aureus rely heavily on their Trx system for survival due to the absence of a GSH-Grx system.

Conclusions:

The Trx system is essential for cellular redox homeostasis and has distinct characteristics in bacteria compared to mammals.
The essentiality of the Trx system in certain pathogenic bacteria presents a promising target for novel antimicrobial therapies.