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Luis Eduardo Soares Netto Versão em português
Advisor do the General Coordination – Biological Sciences 2
Graduated and licensed in Biological Sciences from the University of São Paulo (1986) and PhD in mselves against the toxic effects of free radicals and related species, with an Biological Sciences (Biochemistry) from the University of São Paulo (1992) under the guidance of Dr. Ohara Augusto. He carried out a postdoctoral program at the NIH in collaboration with Dr. Earl Stadtman (1992-1996), where his studies contributed to the elucidation of the enzymatic activity of peroxiredoxins, antioxidant proteins central in the metabolism of H2O2 and of other peroxides. Since 2008, he has been a full professor at the Department of Genetics and Evolutionary Biology at the Institute of Biosciences at the University of São Paulo. Between 2013 and 2017, he served as the Head of the Department of Genetics and Evolutionary Biology at the same institute. He was a member of the Advisory Board of the Society for Redox Biology and Medicine (2013-2018). He is currently a member of the management committee of CEPID Redoxoma and of the editorial board of Free Radical Biology and Medicine.
His research focuses on the mechanisms by which cells defend the emphasis on peroxiredoxins. His studies concentrate on the chemistry and redox biology of thiols such as thioredoxin, glutaredoxin, peroxiredoxin and glutathione. Saccharomyces cerevisiae has been used as a model, exploring collections of thousands of genetically modified strains. One of the highlights of his research is the discovery of the reduction of 1-Cys peroxiredoxins by ascorbate (vitamin C), breaking the paradigm that these proteins are thiol-specific antioxidants.
The antioxidant defense mechanisms of pathogenic bacteria, especially Xylella fastidiosa, and Chromobacterium violaceum and Pseudomonas aeruginosa, have also been studied, and the role of a new class of antioxidant enzymes, called Ohr (“Organic Hydroperoxide Resistance protein”), has been characterized for the first time. These enzymes are central in the response of bacteria to stresses induced by fatty acid-derived peroxides and peroxynitrite. As animals and plants generate oxidants in an attempt to inhibit infection by pathogens, Ohr may play an important role in the pathogenicity of bacteria. In this way, it also carries out analysis of the structures of antioxidant proteins such as Ohr, having so far deposited coordinates in the Protein Data Bank for sixteen protein structures.