Abstract
Here we isolated and characterized two genes ( slr1171, slr1992) designated gpx-1 and gpx-2, respectively, encoding glutathione peroxidase (GPX)-like proteins (Gpx-1, Gpx-2) from Synechocystis PCC 6803. The deduced amino acid sequences for gpx-1 and gpx-2 showed high similarity to those of GPX-like proteins from higher plants and mammalian GPXs, respectively. Surprisingly, both recombinant proteins in Escherichia coli were able to utilize NADPH, but not reduced glutathione, as an electron donor and unsaturated fatty acid hydroperoxides or alkyl hydroperoxides as an acceptor. It seems accurate to refer to Gpx-1 and Gpx-2 as NADPH-dependent GPX-like proteins that serve as a new defense system for the reduction of unsaturated fatty acid hydroperoxides.
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