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Redox Reactions

Redox Reactions

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...

Redox Reactions

Redox Reactions

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...

Redox Titration: Overview

Redox Titration: Overview

Redox titration is a chemical analysis technique used to determine the concentration of an unknown substance by measuring the electron transfer in a redox (reduction-oxidation) reaction. The process involves gradually adding a titrant with a known concentration of an oxidizing or reducing agent, to the analyte, the solution with an unknown concentration, until reaching the endpoint, which indicates the completion of the reaction between the two substances. Ensuring the analyte is in a single...

Redox Equilibria: Overview

Redox Equilibria: Overview

A reduction-oxidation reaction is commonly called a redox reaction. In a redox reaction, electrons are transferred from one species to another rather than being shared between or among atoms. The reducing agent or reductant is the species that loses electrons and gets oxidized in the process. The species that gains electrons and gets reduced in the process is the oxidizing agent or oxidant. Redox reactions are represented as two separate equations called half-reactions, where one equation...

Redox Titration: Other Oxidizing and Reducing Agents

Redox Titration: Other Oxidizing and Reducing Agents

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...

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Related Experiment Video

Updated: May 28, 2026

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

Published on: March 24, 2012

Using quantitative redox proteomics to dissect the yeast redoxome.

Nicolas Brandes¹, Dana Reichmann¹, Heather Tienson¹

¹Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109.

The Journal of Biological Chemistry

|October 7, 2011

Summary

Understanding the yeast redoxome is key to predicting how organisms respond to oxidative stress. This study mapped protein thiol oxidation, revealing that redox sensitivity doesn't always predict peroxide sensitivity, highlighting complex regulation.

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Published on: March 24, 2012

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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

Area of Science:

Biochemistry
Molecular Biology
Cellular Physiology

Background:

The redoxome, comprising proteins regulated by cysteine thiol oxidation, is crucial for understanding organismal responses to changing redox conditions.
Knowledge of the redoxome is essential for predicting physiological effects of altered oxidant levels.

Purpose of the Study:

To quantitatively determine the in vivo thiol oxidation status of proteins in Saccharomyces cerevisiae using the OxICAT method.
To investigate how sublethal hydrogen peroxide (H2O2) treatment affects protein thiol modifications and cellular pathways.
To explore the relationship between steady-state oxidation levels, peroxide sensitivity, and the predictive power of redox sensitivity for thiol modifications.

Main Methods:

Application of the quantitative redox proteomic method, OxICAT (Oxidation in vivo with Carbonyls And Thiols).
Analysis of thiol oxidation status in approximately 300 proteins across various cellular compartments in Saccharomyces cerevisiae.
Treatment of yeast with sublethal hydrogen peroxide (H2O2) concentrations to assess protein thiol modifications.

Main Results:

A significant number of cytosolic and mitochondrial proteins exhibit partial thiol oxidation during exponential growth.
Sublethal H2O2 treatment induced substantial thiol modifications in 41 proteins, impacting pathways related to oxidative stress resistance.
Redox sensitivity of protein thiols was found not to predict their sensitivity to peroxide treatment.

Conclusions:

Prevailing redox conditions dynamically regulate central cellular pathways by fine-tuning protein thiol oxidation status and activity.
The reactivity of protein thiols to changing peroxide levels is influenced by complex thermodynamic and kinetic parameters.
De novo identification of peroxide-sensitive protein thiols is indispensable for accurate prediction of thiol modifications and cellular responses.