ArticleProtein science : a publication of the Protein Society2022
Characterization of the glutathione-dependent reduction of the peroxiredoxin 5 homolog PfAOP from Plasmodium falciparum.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- HAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Mechanism of glutathionylation of the active site thiols of peroxiredoxin 2.The Journal of biological chemistry · 2025Article
- Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with glutathione for protein disulfide reduction.Nature communications · 2024Article
- Characterization of the glutathione-dependent reduction of the peroxiredoxin 5 homolog PfAOP from Plasmodium falciparum.Protein science : a publication of the Protein Society · 2022Article
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3 authors.
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Abstract
Peroxiredoxins use a variety of thiols to rapidly reduce hydroperoxides and peroxynitrite. While the oxidation kinetics of peroxiredoxins have been studied in great detail, enzyme-specific differences regarding peroxiredoxin reduction and the overall rate-limiting step under physiological conditions often remain to be deciphered. The 1-Cys peroxiredoxin 5 homolog PfAOP from the malaria parasite Plasmodium falciparum is an established model enzyme for glutathione/glutaredoxin-dependent peroxiredoxins. Here, we reconstituted the catalytic cycle of PfAOP in vitro and analyzed the reaction between oxidized PfAOP and reduced glutathione (GSH) using molecular docking and stopped-flow measurements. Molecular docking revealed that oxidized PfAOP has to adopt a locally unfolded conformation to react with GSH. Furthermore, we determined a second-order rate constant of 6 × 10
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