Glutathione reductase (Plasmodium falciparum) (PfGR)

Glutathione reductase from Plasmodium falciparum (PfGR) is a homodimeric flavoenzyme central to the parasite's antioxidant defense, catalyzing the NADPH-dependent reduction of oxidized glutathione (GSSG) to reduced glutathione (GSH). This maintains redox balance, allowing the parasite to withstand oxidative stress encountered in the host. Its structural divergence from the human enzyme—especially at the ligand-binding and intersubunit sites—makes PfGR an attractive target for antimalarial therapy. Selective inhibition impairs the parasite's ability to detoxify reactive oxygen species, contributing to parasite death[1][2][3][6][7].

Other names

Glutathione reductaseGRPfGR

Inhibition of glutathione reductase disrupts reduction of glutathione disulfide (GSSG) to reduced glutathione (GSH), impairing the parasite's antioxidant defenses[2][3][7].