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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...
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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...
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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.
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Energy production within a cell involves many coordinated chemical pathways. Most of these pathways are combinations of oxidation and reduction reactions, which occur at the same time. An oxidation reaction strips an electron from an atom in a compound, and the addition of this electron to another compound is a reduction reaction. Because oxidation and reduction usually occur together, these pairs of reactions are called redox reactions.
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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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Interplay between redox and protein homeostasis.

Diogo R Feleciano1, Kristin Arnsburg1, Janine Kirstein1

  • 1Leibniz-Institut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. , Berlin, Germany.

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Summary
This summary is machine-generated.

Cellular compartments have distinct redox environments affecting protein folding. This review explores thioredoxin superfamily members and chaperones in C. elegans, linking redox and protein homeostasis.

Keywords:
ERO-1PDIagingchaperonesendoplasmic reticulumproteostasisredox homeostasisthioredoxintrx-domainunfolded protein response

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Eukaryotic cells possess distinct subcellular compartments with varying redox potentials, influencing protein folding and stability.
  • The endoplasmic reticulum is oxidizing, while the cytosol, nucleus, and mitochondria are reducing, impacting disulfide bond formation.
  • Protein homeostasis (proteostasis) networks must adapt to these compartmental redox properties, involving chaperones and the thioredoxin superfamily.

Purpose of the Study:

  • To review the roles of thioredoxin superfamily members and chaperones in Caenorhabditis elegans.
  • To highlight the interplay between redox environments and protein homeostasis in C. elegans.
  • To discuss recent advancements in assessing cellular redox states in vivo and in vitro.

Main Methods:

  • Literature review focusing on C. elegans.
  • Analysis of the functions of thioredoxin superfamily members and chaperones.
  • Examination of methodological developments for redox state assessment.

Main Results:

  • Thioredoxin superfamily members and chaperones are crucial for maintaining protein homeostasis across different redox environments in C. elegans.
  • Specific redox properties of cellular compartments dictate protein folding pathways.
  • New methods enable better in vivo and in vitro assessment of redox states.

Conclusions:

  • The redox and proteostasis networks in C. elegans are complex and interconnected.
  • Understanding these networks is vital for comprehending cellular function and dysfunction.
  • Further research utilizing advanced methodologies will deepen insights into redox biology and protein folding.