Abstract
Our cellular macromolecules are continuously damaged by harmful reactive oxygen species (ROS) which are produced as natural by-products during intracellular processes (respiration) and by external sources (e.g. UV-irradiation and cigarette smoke). If these damages are not prevented and/or repaired, they will promote oxidative damages which ultimately can lead to development of cancer, neurological diseases and premature aging. Fortunately, the presence of redox scavenging systems and DNA repair machineries reduces the extent of induced damages; however, the underlying molecular mechanisms of these systems are largely unknown. Here we describe the cloning and expression tests of one peroxidase – Dye decolorizing peroxidase - from the extremely radiation and desiccation resistant bacterium Deinococcus radiodurans, in order to determine its potential role as part of the antioxidant defense system. The enzyme was overexpressed in E.coli, purified, crystallised and characterized by UV-vis and Resonance Raman spectroscopies. Our aim is to perform structure/function analysis of this protein and in a long term prespective, improve our understanding of oxidative stress related human diseases.
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