Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Sulfur Assimilation01:20

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...
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...
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...
Protein Modifications in the RER01:26

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 Formation01:22

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

Spectroelectrochemical Studies of CTAB Adsorbed on Gold Surfaces in Perchloric Acid.

Langmuir : the ACS journal of surfaces and colloids·2023
Same author

Dragon 1 Protocol Manuscript: Training, Accreditation, Implementation and Safety Evaluation of Portal and Hepatic Vein Embolization (PVE/HVE) to Accelerate Future Liver Remnant (FLR) Hypertrophy.

Cardiovascular and interventional radiology·2022
Same author

A nearby transiting rocky exoplanet that is suitable for atmospheric investigation.

Science (New York, N.Y.)·2021
Same author

A giant exoplanet orbiting a very-low-mass star challenges planet formation models.

Science (New York, N.Y.)·2019
Same author

A candidate super-Earth planet orbiting near the snow line of Barnard's star.

Nature·2018
Same author

Acute kidney injury in critically burned patients resuscitated with a protocol that includes low doses of Hydroxyethyl Starch.

Annals of burns and fire disasters·2017

Related Experiment Video

Updated: Jul 15, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

Monothiol glutaredoxins: a common domain for multiple functions.

E Herrero1, M A de la Torre-Ruiz

  • 1Departament de Ciències Mèdiques Bàsiques, IRBLLEIDA, Universitat de Lleida, Montserrat Roig 2, Lleida, Spain. enric.herrero@cmb.udl.es

Cellular and Molecular Life Sciences : CMLS
|April 7, 2007
PubMed
Summary

Monothiol glutaredoxins are vital protein redox regulators found across life. These enzymes, like yeast Grx3/Grx4 and human PICOT, participate in diverse cellular functions including iron metabolism and kinase activity.

More Related Videos

Live Imaging of the Mitochondrial Glutathione Redox State in Primary Neurons using a Ratiometric Indicator
07:47

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

Published on: October 20, 2021

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
08:57

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

Published on: February 24, 2018

Related Experiment Videos

Last Updated: Jul 15, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

Live Imaging of the Mitochondrial Glutathione Redox State in Primary Neurons using a Ratiometric Indicator
07:47

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

Published on: October 20, 2021

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
08:57

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

Published on: February 24, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Monothiol glutaredoxins, characterized by the CGFS active site, are prevalent in prokaryotes and eukaryotes.
  • They exist in two subclasses: single-domain and hybrid structures with a thioredoxin-like region.
  • The Saccharomyces cerevisiae Grx5 protein is crucial for iron-sulfur cluster biogenesis.

Purpose of the Study:

  • To explore the diverse cellular roles of monothiol glutaredoxins.
  • To investigate the functions of specific yeast glutaredoxins (Grx3, Grx4) and their human homologue (PICOT).
  • To understand the common structural and functional mechanisms of these protein redox regulators.

Main Methods:

  • Comparative analysis of glutaredoxin structures and functions across different species.
  • Investigating the role of yeast Grx3 and Grx4 in regulating the iron uptake transcriptional activator Aft1.
  • Examining the function of the human PICOT protein in protein kinase C regulation.

Main Results:

  • Yeast Grx3 and Grx4 modulate the transcriptional activator Aft1, impacting iron uptake.
  • Human PICOT, a homologue of Grx3/Grx4, regulates protein kinase C activity.
  • Monothiol glutaredoxins share a conserved structural motif and biochemical mechanism.

Conclusions:

  • Monothiol glutaredoxins are versatile protein redox regulators with diverse cellular functions.
  • Homologues like yeast Grx3/Grx4 and human PICOT highlight conserved roles and species-specific adaptations.
  • These proteins are critical in processes ranging from iron homeostasis to signal transduction.