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Related Concept Videos

Redox Reactions01:27

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 Reactions01:24

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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Redox Equilibria: Overview01:23

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...
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...

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Related Experiment Video

Updated: Jun 24, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Redox-regulated chaperones.

Caroline Kumsta1, Ursula Jakob

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

Biochemistry
|April 17, 2009
PubMed
Summary
This summary is machine-generated.

Redox regulation allows stress proteins like Hsp33 and peroxiredoxins to quickly respond to oxidative stress. Their function as molecular chaperones is controlled by the oxidation of specific cysteines, protecting cells from damage.

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Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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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 Stress Response

Background:

  • Oxidative stress poses a significant threat to cellular integrity, leading to protein unfolding and aggregation.
  • Molecular chaperones are crucial for maintaining protein homeostasis under stress conditions.
  • Redox regulation offers a rapid mechanism for modulating chaperone activity.

Purpose of the Study:

  • To review the redox regulation of two major classes of chaperones: bacterial Hsp33 and eukaryotic 2-Cys peroxiredoxins.
  • To elucidate how redox-sensitive cysteines control chaperone function in response to oxidative stress.
  • To highlight the role of redox regulation in cellular protection against reactive oxygen species.

Main Methods:

  • Comparative analysis of Hsp33 and 2-Cys peroxiredoxins.
  • Discussion of redox-sensitive cysteine modifications (disulfide bond formation, sulfinic acid formation).
  • Review of literature on chaperone activation mechanisms under oxidative stress.

Main Results:

  • Hsp33 activation involves oxidative stress-induced disulfide bond formation, leading to partial unfolding and exposure of a high-affinity binding site for unfolded proteins.
  • Eukaryotic 2-Cys peroxiredoxins, upon oxidative stress, undergo sulfinic acid formation, converting them into molecular chaperones.
  • Both systems demonstrate rapid adaptation to oxidative stress via reversible cysteine modifications.

Conclusions:

  • Redox regulation of chaperones provides an immediate response to oxidative stress, essential for cell survival.
  • Hsp33 is vital for bacterial protection against severe oxidative insults like hypochlorite treatment.
  • Reversible cysteine modifications are a key strategy for proteins to adapt to oxidative environments and prevent cell death.