Related Experiment Video
Updated: Jul 2, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
Enzymes or redox couples? The kinetics of thioredoxin and glutaredoxin reactions in a systems biology context
Ché S Pillay1, Jan-Hendrik S Hofmeyr, Brett G Olivier
1Triple-J Group for Molecular Cell Physiology, Department of Biochemistry, Stellenbosch University, ZA-7602 Matieland, Stellenbosch, South Africa.
Abstract:
Systems biology approaches, such as kinetic modelling, could provide valuable insights into how thioredoxins, glutaredoxins and peroxiredoxins (here collectively called redoxins), and the systems that reduce these molecules are regulated. However, it is not clear whether redoxins should be described as redox couples (with redox potentials) or as enzymes (with Michaelis-Menten parameters) in such approaches. We show that in complete redoxin systems, redoxin substrate saturation and other purported enzymatic behaviours result from limitations in the redoxin redox cycles in these systems. Michaelis-Menten parameters are therefore inappropriate descriptors of redoxin activity; data from redoxin kinetic experiments should rather be interpreted in terms of the complete system of reactions under study. These findings were confirmed by fitting kinetic models of the thioredoxin and glutaredoxin systems to in vitro datasets. This systems approach clarifies the inconsistencies with the descriptions of redoxins and emphasizes the roles of redoxin systems in redox regulation.
Related Concept Videos
Redox Reactions
Redox Reactions
Redox Equilibria: Overview
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...
Oxidation and Reduction of Organic Molecules
The removal of an electron from a molecule, results in a...
Electron Transport Chain: Complex III and IV

