Characterization of the glutathione-dependent reduction of the peroxiredoxin 5 homolog PfAOP from Plasmodium falciparum.

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 reac

SUBMITTER: Schumann R 

PROVIDER: S-EPMC8994508 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature