Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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 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...

Electron Transport Chain: Complex III and IV

Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...

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...

Protein Modifications in the RER

Protein Modifications in the RER

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 sequences.

Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation

Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation

Glutathione, a tripeptide made up of glutamate, cysteine, and glycine, is a critical player in the detoxification of drugs and xenobiotics via a process known as glutathione conjugation or mercapturic acid formation. This phase II biotransformation reaction involves the covalent binding of glutathione to a drug or its metabolite, enhancing the compound's water solubility and enabling its excretion.
Several distinctive characteristics distinguish glutathione conjugation from other phase II...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Oxidative and nitrosative damage in multiple sclerosis.

Current opinion in neurology·2026

Same author

Redox homeostasis in ferroptosis and aging: a causal role for fard-1 and dhs-25 in Caenorhabditis elegans.

Redox biology·2025

Same author

Fumarate-based drugs protect against neuroinflammation via upregulation of anti-ferroptotic pathways.

Journal of neuroinflammation·2025

Same author

Flecainide mediated sodium channel blockade enhances blood brain barrier integrity and promotes neuroprotection in neuroinflammation.

Scientific reports·2025

Same author

The thioredoxin-like and one glutaredoxin domain are required to rescue the iron-starvation phenotype of HeLa GLRX3 knock out cells.

FEBS letters·2025

Same author

Impact of nephrotoxins and oxidants on survival and transport function of hiPSC-derived renal proximal tubular cells.

Archives of toxicology·2025

Same journal

Cumulative Contents.

Biochimica et biophysica acta·2020

Same journal

Molecular Basis of Disease Cumulative Contents.

Biochimica et biophysica acta·2020

Same journal

General Subjects Cumulative Contents.

Biochimica et biophysica acta·2020

Same journal

Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

Biochimica et biophysica acta·2019

Same journal

Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

Biochimica et biophysica acta·2019

Same journal

Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

Biochimica et biophysica acta·2019

See all related articles

Search research articles

Related Experiment Video

Updated: Jul 3, 2026

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Published on: February 24, 2018

Glutaredoxin systems.

Christopher Horst Lillig¹, Carsten Berndt, Arne Holmgren

¹The Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17177 Stockholm, Sweden.

Biochimica Et Biophysica Acta

|July 16, 2008

Summary

This summary is machine-generated.

Glutaredoxins regulate cellular redox balance and signaling. Recent discoveries reveal new roles in iron metabolism and iron-sulfur cluster biosynthesis, impacting human health and disease.

More Related Videos

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

Live Imaging of the Mitochondrial Glutathione Redox State in Primary Neurons using a Ratiometric Indicator

Live Imaging of the Mitochondrial Glutathione Redox State in Primary Neurons using a Ratiometric Indicator

Published on: October 20, 2021

Related Experiment Videos

Last Updated: Jul 3, 2026

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Published on: February 24, 2018

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

Live Imaging of the Mitochondrial Glutathione Redox State in Primary Neurons using a Ratiometric Indicator

Live Imaging of the Mitochondrial Glutathione Redox State in Primary Neurons using a Ratiometric Indicator

Published on: October 20, 2021

Area of Science:

Biochemistry
Cell Biology
Molecular Medicine

Background:

Glutaredoxins are key enzymes utilizing glutathione to regulate cellular redox state.
They are involved in critical cellular processes including redox-dependent signaling and protein S-glutathionylation.
Dysregulation of glutaredoxin activity is implicated in various diseases, including cancer and neurodegeneration.

Purpose of the Study:

To provide a comprehensive overview of recent advancements in glutaredoxin research.
To highlight novel functions of glutaredoxin systems beyond traditional redox regulation.
To focus on the implications of these discoveries for human health and disease.

Main Methods:

Literature review of recent scientific publications.
Synthesis of findings from studies on glutaredoxin systems and functions.
Analysis of the connection between glutaredoxins, iron metabolism, and iron-sulfur cluster biosynthesis.

Main Results:

Identification of new glutaredoxin systems and their diverse functions.
Elucidation of unexpected roles in iron metabolism and iron-sulfur cluster biosynthesis.
Demonstration of glutaredoxins' involvement in a broader spectrum of physiological and pathological conditions.

Conclusions:

Recent discoveries have significantly expanded our understanding of glutaredoxin functions.
Glutaredoxins are crucial regulators of cellular redox homeostasis with emerging roles in iron metabolism.
These findings offer new perspectives for therapeutic strategies targeting diseases associated with glutaredoxin dysfunction.