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Aerobic organisms are characterized by the use of molecular oxygen as the final electron acceptor in the process known as respiration. In the inner membrane of mitochondria the four respiratory complexes transport the electrons and protons from FADH and NAD(P)H to oxygen and produce H2O. This mechanism is coupled to energy generation, but incomplete reduction of O2 causes the appearance of reactive oxygen species (ROS) such as hydrogen peroxide (H2O2), the hydroxyl radical (OH-) and the superoxide anion (O2.-). ROS are highly reactive in the cell and interact with nucleic acids, proteins and lipids, thus causing a wide spectrum of damages. Increase in steady state ROS level leads to oxidative stress (Lushchak, 2011) and stimulates defence systems. Along evolution of aerobic organisms diverse antioxidant strategies were developed. Many proteins have the function of removing ROS or are able to correct the damage caused by them. Glutathione (GSH), a tripeptide formed by cysteine, glutamic acid and glycine, is the major non-protein thiolbased redox buffer present in the cell (Penninckx, 2002; Perrone et al., 2005). Glutathione is synthesized in its reduced form and transformed to the oxidized form (GSSG) by the formation of one inter-molecular disulfide bond. The principal function of glutathione is to maintain the intracellular redox balance, reducing oxidized molecules and detoxifying ROS, xenobiotics and heavy metals (Grant et al., 1996b; Yu & Zhou, 2007). In fact, for long time the GSH/GSSG ratio was used to describe the redox state of the cell. GSH binds to and directly reduces oxidized molecules, but more often GSH is used as a donor of reducing equivalents to other antioxidant enzymes, like glutaredoxins, glutathione peroxidases and glutathione transferases (Avery & Avery, 2001; Garcera et al., 2006; Lillig et al., 2008).

The Yeast Genes ROX1, IXR1, SKY1 and Their Effect upon Enzymatic Activities Related to Oxidative Stress