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

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...

Sulfur Assimilation

Sulfur Assimilation

Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...

The Supercomplexes in the Crista Membrane

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...

Electron Transport Chain: Complex I and II

Electron Transport Chain: Complex I and II

The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...

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...

Complexation Equilibria: The Chelate Effect

Complexation Equilibria: The Chelate Effect

In complexation reactions, metal atoms or cations interact with ligands to form donor-acceptor adducts called metal complexes. Ligands that bind through one donor site are monodentate, ligands with two donor sites are bidentate, and those with more than two donor sites are polydentate ligands. For example, ethylene diamine is a bidentate ligand that binds through two nitrogen donor atoms, forming a five-membered ring. EDTA is a polydentate ligand that binds through four oxygen and two nitrogen...

You might also read

Related Articles

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

Sort by

Same author

Structural and sequence basis for substrate selection in the cellular trafficking of Fe-S clusters, hemes and glutathione-complexed metals through membrane transporters.

Journal of inorganic biochemistry·2025

Same author

Understanding the Thermodynamics of Magnesium Binding to RNA Structural Motifs.

Life (Basel, Switzerland)·2024

Same author

Influence of the Weak Nuclear Force on Metal-Promoted Autocatalytic Strecker Synthesis of Amino Acids: Formation of a Chiral Pool of Precursors for Prebiotic Peptide and Protein Synthesis.

Life (Basel, Switzerland)·2024

Same author

Bidirectional Catalysis Disintegration and Mineral Polymerization via Endogenous Iron(III) from Iron-Rich Sludge in Synergy with Waste Incineration Fly Ash.

ACS omega·2023

Same author

Association of tirofiban with improvement of functional outcomes of direct thrombectomy for acute anterior circulation occlusion: a retrospective, nonrandomized, multicenter, real-world study.

Neurosurgical focus·2023

Same author

Ethyl Acetate Fraction from Hedyotis Diffusa Plus Scutellaria Barbata Inhibits the Progression of Breast Cancer <i>via</i> Targeting LMO1 and AKT/Mtor Signaling Pathway.

Combinatorial chemistry & high throughput screening·2023

Search research articles

Related Experiment Video

Updated: May 21, 2026

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

Glutathione complexed Fe-S centers.

Wenbin Qi¹, Jingwei Li, C Y Chain

¹Ohio State Biochemistry Program, The Ohio State University, 100 West 18th Avenue, Columbus, Ohio 43210, USA.

Journal of the American Chemical Society

|June 13, 2012

Summary

This summary is machine-generated.

Glutathione alone can stabilize iron-sulfur clusters. This finding reveals a new role for glutathione in cellular iron-sulfur cluster biosynthesis, independent of glutaredoxins.

More Related Videos

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 Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins

The Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins

Published on: December 13, 2013

Related Experiment Videos

Last Updated: May 21, 2026

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

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 Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins

The Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins

Published on: December 13, 2013

Area of Science:

Biochemistry
Molecular Biology
Bioinorganic Chemistry

Background:

Glutathione (γ-glutamyl-cysteinyl-glycine, GSH) is a crucial thiol-containing peptide found at high concentrations within cells.
Recent studies suggest glutaredoxins (Grx) mediate iron-sulfur cluster formation using glutathione as a ligand.
The precise role of glutathione in iron-sulfur cluster biosynthesis remains an active area of research.

Purpose of the Study:

To investigate the direct interaction between glutathione and iron-sulfur clusters.
To characterize the structure and stability of glutathione-bound iron-sulfur complexes.
To elucidate the mechanism of iron-sulfur cluster formation involving glutathione.

Main Methods:

Spectroscopic analysis (optical, redox, Mössbauer, NMR) to characterize the complex.
In vitro assays using the Fe-S assembly protein ISU.
Iron and sulfide ion titration in the presence of glutathione.

Main Results:

Glutathione alone can coordinate and stabilize an [Fe(2)S(2)] cluster under physiological conditions.
The resulting complex, [Fe(2)S(2)](GS)(4), exhibits distinct spectroscopic properties.
The ISU protein catalyzes the formation of [Fe(2)S(2)](GS)(4), which can reversibly exchange its iron-sulfur core with apo ISU and free glutathione.

Conclusions:

Glutathione directly participates in the stabilization of iron-sulfur clusters.
This interaction provides a novel pathway for cellular iron-sulfur cluster biosynthesis.
The findings expand our understanding of the multifaceted roles of glutathione in cellular processes.