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2014
Journal Article
Titel
A novel natural NADH and NADPH dependent glutathione reductase as tool in biotechnological applications
Abstract
The antioxidant glutathione (GSH) is an important reducing agent in cell physiology. Glutathione reductases (GR) of humans and higher organisms convert oxidized glutathione (GSSG) to two reduced GSH molecules under consumption of the co-factor NADPH. GSH acts as an antioxidant eliminating reactive oxygen species in the cell. We found a novel GR being able to accept both NADPH and much cheaper NADH for GSSG reduction. For the first time we produced it in E. coli and purified active GR from Allochromatium vinosum, determined its Km-values for NADH (0.026 mM) and NADPH (0.309 mM), as well as its temperature optimum (20 °C) and pH optimum (pH 8). Since numerous bio-diagnostic assays and enzymatic processes are dependent on GRs the possibility to use a cheaper co-substrate could help to overcome cost limitations in future.