Related Experiment Video
Updated: Jul 5, 2026

Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors
Published on: February 7, 2018
The dual functions of thiol-based peroxidases in H2O2 scavenging and signaling
Simon Fourquet1, Meng-Er Huang, Benoit D'Autreaux
1CEA, DSV, IBITECS, Laboratoire Stress Oxydants et Cancer, CEA-Saclay, Gif-sur-Yvette France.
Abstract:
Thiol-based peroxidases consist of the peroxiredoxins (Prx) and the related glutathione peroxidase (GPx)-like enzymes. Their catalytic function is to reduce peroxides by using the reactivity of the cysteine residue, and their presumed primary physiologic role is to protect living organisms from peroxide toxicity. However, as peroxide-metabolizing enzymes, they also regulate hydrogen peroxide (H2O2) signaling. We review here enzymatic and biochemical attributes of thiol peroxidases that specify both distinctive peroxide-scavenging functions and the property of regulating H2O2 signaling. We then discuss possible thiol peroxidase physiologic functions, based on selected observations made in microorganisms and mammals.
Related Concept Videos
Oxidation of Phenols to Quinones
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...
Preparation and Reactions of Thiols
Peroxisomes
Peroxisomes
Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide
Radical Autoxidation

