Redox Regulation in Plant Systems

Redox regulation underpins the dynamic control of plant metabolism, signalling and stress responses by orchestrating reversible oxidation–reduction of protein cysteine residues. Central to this network are reactive oxygen species (ROS), which serve both as damaging agents at elevated levels and as signalling intermediates at controlled concentrations. Plants maintain redox homeostasis through a suite of oxidoreductases, notably thioredoxins (Trxs), glutaredoxins and peroxiredoxins (Prxs), which modulate the activity of key metabolic enzymes and regulatory proteins. In chloroplasts, light-driven electron flow generates reduced ferredoxin and NADPH that fuel the ferredoxin–thioredoxin and NADPH–thioredoxin reductase C (NTRC) systems, enabling rapid activation of Calvin–Benson cycle enzymes and other biosynthetic pathways upon illumination. Conversely, oxidative signals and peroxiredoxin-mediated thiol oxidation serve to inactivate these enzymes during dark periods or stress conditions, preventing futile metabolism. Beyond photosynthesis, redox regulation extends to responses against abiotic stresses such as cold and drought, where redox-sensitive transcription factors and signalling proteins coordinate adaptive gene expression. Recent advances in redox proteomics have illuminated the vast repertoire of thiol-modified proteins, revealing intricate crosstalk between reductive and oxidative pathways that fine-tune plant growth, development and stress resilience on a global scale.

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Redox Regulation in Plant Systems publication trend

The graph below shows the total number of articles in redox regulation in plant systems across all publications each year (not limited to Nature Index journals).

Technical terms

Redox regulation: Control of protein function and signalling via reversible oxidation and reduction of thiol groups in cysteine residues.

Thioredoxin (Trx): Small oxidoreductase proteins that reduce disulfide bonds in target enzymes, modulating their activity in response to cellular redox state.

Peroxiredoxin (Prx): Peroxide-detoxifying enzymes that catalyse reduction of hydrogen peroxide and serve as thioredoxin oxidases to promote protein re-oxidation.

Reactive oxygen species (ROS): Chemically reactive molecules derived from oxygen, including hydrogen peroxide and superoxide, functioning as both stress agents and signalling mediators.

NADPH-thioredoxin reductase C (NTRC): A bifunctional chloroplast enzyme combining thioredoxin reductase and thioredoxin domains, central to maintaining thiol-redox balance under light and stress conditions.

References

1. The impact of light and thioredoxins on the plant thiol-disulfide proteome. Plant Physiology (2024).
2. The Functional Relationship between NADPH Thioredoxin Reductase C, 2-Cys Peroxiredoxins, and m-Type Thioredoxins in the Regulation of Calvin–Benson Cycle and Malate-Valve Enzymes in Arabidopsis. Antioxidants (2023).
3. Ketocarotenoid production in tomato triggers metabolic reprogramming and cellular adaptation: The quest for homeostasis. Plant Biotechnology Journal (2023).
4. The chloroplast 2-cysteine peroxiredoxin functions as thioredoxin oxidase in redox regulation of chloroplast metabolism. eLife (2018).
5. Reactive Oxygen Species and the Redox-Regulatory Network in Cold Stress Acclimation. Antioxidants (2018).