Abstract
Glutathione peroxidase (GPX)-like proteins (GPX-1 and GPX-2) of Synechocystis PCC 6803 (S. PCC 6803) reduce unsaturated fatty acid hydroperoxides using NADPH, but not reduced glutathione (GSH), as an electron donor. Here, we generated transgenic Arabidopsis plants overexpressing S. PCC 6803 GPX-2 in the cytosol (AcGPX2) or chloroplasts (ApGPX2). The activities toward α-linolenic acid hydroperoxide in ApGPX2 and AcGPX2 plants were 6.5–11.5 and 8.2–16.3 nmol min−1 mg protein−1, respectively, while no activity (