Modulating protein function through reversible oxidation: Redox-mediated processes in plants revealed through proteomics
Related Experiment Video
Updated: May 16, 2026

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
Published on: March 24, 2012
Natalia V Bykova1, Christof Rampitsch
1Cereal Research Centre, Agriculture and AgriFood Canada, 195 Dafoe Road, Winnipeg, Manitoba, Canada. bykovan@agr.gc.ca
Abstract:
It has been clearly demonstrated that plants redox control can be exerted over virtually every cellular metabolic pathway affecting metabolic homeostasis and energy balance. Therefore, a tight link exists between cellular/compartmental steady-state redox level and cellular metabolism. Proteomics offers a powerful new way to characterize the response and regulation of protein oxidation in different cell types and in relation to cellular metabolism. Compelling evidence revealed in proteomics studies suggests the integration of the redox network with other cellular signaling pathways such as Ca(2+) and/or protein phosphorylation, jasmonic, salicylic, abscisic acids, ethylene, and other phytohormones. Here we review progress in using the various proteomics techniques and approaches to answer biological questions arising from redox signaling and from changes in redox status of the cell. The focus is on reversible redox protein modifications and on three main processes, namely oxidative and nitrosative stress, defense against pathogens, cellular redox response and regulation, drawing on examples from plant redox proteomics studies.
Related Concept Videos
Redox Reactions
Redox Reactions
Protein Modifications in the RER
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.
Oxidation and Reduction of Organic Molecules
The removal of an electron from a molecule, results in a...
The Calvin Benson Cycle
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.

