New finding: Peroxiredoxins form hybrid complexes

by | Mar 11, 2026 | Health, Research

Researchers from Saarland University, the Rhineland-Palatinate University of Technology Kaiserslautern-Landau, the VIB-VUB Brussels and other institutions have shown that peroxiredoxins – important protective enzymes in cells – can be combined more flexibly than previously assumed.

Peroxiredoxins regulate the content of peroxides such as hydrogen peroxide and protect cells from oxidative stress. For more than two decades, it was considered certain that these enzymes consist exclusively of ten identical protein units and form doughnut-shaped complexes. However, the new study shows that cells can mix two different variants of the enzyme and thus create hybrid protein complexes.

Peroxiredoxin heteroassemblies are distributed across a negative-contrast electron microscopy grid. A heterodecamer stands out sharply and illustrates the structural diversity of cellular antioxidant enzymes. | Copyright: Joris Messens
Peroxiredoxin heteroassemblies are distributed across a negative-contrast electron microscopy grid. A heterodecamer stands out sharply and illustrates the structural diversity of cellular antioxidant enzymes. | Copyright: Joris Messens

The combination of two building blocks with different properties results in a high molecular diversity of comparatively few basic elements. Biochemical and imaging analyses showed that this mixture occurs in very different organisms – from yeasts and humans to plants and parasites.

The researchers speak of a “molecular Lego strategy” that enables cells to precisely coordinate stress reactions and cellular signaling pathways. The new understanding of mixed peroxiredoxin complexes could explain how cells adapt to oxygen-rich environments. In addition, it opens up possible insights into the development of diseases in which the oxidative balance is disturbed, such as aging processes, cancer and metabolic diseases.

Original Paper:

Hetero-oligomerization drives structural plasticity of eukaryotic peroxiredoxins | Nature Chemical Biology

Read Also:

Researchers clarify electron source for peroxiredoxin-6 enzymes – MedLabPortal

RADAR pathway: Discovery of new quality control in peroxisomes – MedLabPortal


Editor: X-Press Journalistenbüro GbR

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