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H2S Is a Potential Universal Reducing Agent for Prx6-Type Peroxiredoxins.

Lukas Lang1, Laura Leiskau1, Lea Bambach1

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|October 1, 2025
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Hydrosulfide ion (HS⁻) is a potent universal electron donor for Prx6-type peroxiredoxins, unlike other agents. This finding opens new avenues for understanding H₂S detoxification and redox signaling pathways.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Redox Biology

Background:

  • Prx6-type peroxiredoxins lack a universal reducing agent, unlike Prx1-type subfamilies.
  • A conserved histidyl residue in Prx6 active sites may hinder reduction by common agents.

Purpose of the Study:

  • To investigate the reduction of Prx6-type peroxiredoxins by the hydrosulfide ion (HS⁻).
  • To elucidate the role of the active-site histidine in Prx6 enzyme reactivity.

Main Methods:

  • Enzymatic assays using oxidized wild-type and mutant PfPrx6 (Plasmodium falciparum) and human PrxVI.
  • Kinetic analysis of reactions with hydrosulfide ion (HS⁻) at pH 7.4.
  • Testing reduction of intermediate species by thioredoxin, glutaredoxin, and glutathione.

Main Results:

  • HS⁻ rapidly reduced oxidized wild-type PfPrx6 and hPrxVI (k₂ > 10⁸ M⁻¹s⁻¹), but not histidyl mutants.
  • The resulting protein-hydropersulfide intermediate reacted further with HS⁻ (k₂ ≈ 10⁴ M⁻¹s⁻¹).
  • Thioredoxin, glutaredoxin, and glutathione did not reduce the hydropersulfide intermediate.

Conclusions:

  • HS⁻ is identified as a highly reactive, potential universal electron donor for Prx6-type enzymes.
  • This discovery is crucial for understanding H₂S detoxification, redox signaling, and persulfide metabolism.