Journal article

Structural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparum

Ian W Boucher, Paul J McMillan, Mads Gabrielsen, Susan E Akerman, James A Brannigan, Claudia Schnick, Andrzej M Brzozowski, Anthony J Wilkinson, Sylke Muller

Molecular Microbiology | WILEY | Published : 2006

Abstract

Plasmodium falciparum possesses a single mitochondrion with a functional electron transport chain. During respiration, reactive oxygen species are generated that need to be removed to protect the organelle from oxidative damage. In the absence of catalase and glutathione peroxidase, the parasites rely primarily on peroxiredoxin-linked systems for protection. We have analysed the biochemical and structural features of the mitochondrial peroxiredoxin and thioredoxin of P. falciparum. The mitochondrial localization of both proteins was confirmed by expressing green fluorescent protein fusions in parasite erythrocytic stages. Recombinant protein was kinetically characterized using the cytosolic ..

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University of Melbourne Researchers