10 March 2026

How Cells Work with “Lego Building Blocks”: New Study Reveals Heterogeneity in Peroxidases

Mikroskopische Aufnahme einer Peroxidase
© Joris MessensPeroxiredoxin hetero-assemblies dot a negative-stain electron microscopy grid, with one heterodecamer in sharp focus, illustrating the structural diversity of cellular antioxidant enzymes.

Scientists from Saarland University, RPTU Kaiserslautern–Landau, VIB-VUB Brussels and collaborating institutions have discovered that important enzymes in our cells, known as peroxiredoxins, can combine more flexibly than previously assumed. The discovery shows how cells create molecular diversity and fine-tune stress responses.

 

Peroxiredoxins have protective and regulatory functions by controlling the levels of peroxides such as hydrogen peroxide. For more than 20 years, researchers assumed that these enzymes form complexes made of ten identical protein units arranged in a donut-like structure. However, the newly published study shows that cells can instead mix two versions of the enzyme, forming hybrid protein complexes.

By combining two building blocks with different properties, cells can form many different protein complexes and thus generate a large variety of molecular structures and functions from only two building blocks. Using biochemical and imaging approaches, the researchers found that this mixing occurs in organisms ranging from yeast to humans, as well as in plants and parasites.

The researchers emphasize that this “molecular Lego strategy” may help cells fine-tune stress responses and signaling pathways. Understanding how these mixed complexes function could provide new insights into how cells adapt to life with oxygen and how diseases arise in which the oxidative balance in the cell is disturbed, including aging, cancer, and metabolic disorders.
 

Study:
“Heterooligomerization drives structural plasticity of eukaryotic peroxiredoxins”, Nature Chemical Biology (https://doi.org/10.1038/s41589-026-02157-6)

Further information:
Bruce Morgan 
Institut für Biochemie
Zentrum für Human- und Molekularbiologie (ZHMB)
Universität des Saarlandes
Email: bruce.morgan(at)uni-saarland.de 

Marcel Deponte 
Vergleichende Biochemie 
Fachbereich Chemie
RPTU Kaiserslautern-Landau
Email: deponte(at)rptu.de 

Joris Messens
VIB-VUB Center for Structural Biology
Brussels
Email: joris.messens(at)vub.be   
 

Mikroskopische Aufnahme einer Peroxidase
© Joris MessensPeroxiredoxin hetero-assemblies dot a negative-stain electron microscopy grid, with one heterodecamer in sharp focus, illustrating the structural diversity of cellular antioxidant enzymes.