Efficiency of superoxide anions in the inactivation of selected dehydrogenases |
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| Authors: | Aleksandra Rodacka Eligiusz Serafin Mieczyslaw Puchala |
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| Affiliation: | 1. Department of Molecular Biophysics, University of Lodz, Banacha 12/16, 90-237 Lodz, Poland;2. Laboratory of Computer and Analytical Techniques, University of Lodz, Banacha 12/16, 90-237 Lodz, Poland;1. Department of Experimental Petrology, Institute of Geological Sciences, University of Wroc?aw, Cybulskiego Street 32, 50-205 Wroclaw, Poland;2. Department of Ecologistic and Environmental Risk Management, Wroc?aw University of Technology, 9 Grunwaldzki Sq., 50-377 Wroc?aw, Poland;1. Division of Geriatrics, Gerontology, and Palliative Medicine, Department of Medicine, UTHSCSA, San Antonio, TX 78229, United States;2. Center for Healthy Aging, UTHSCSA, San Antonio, TX 78229, United States;3. Department of Surgery, Thomas E. Starzl Transplantation Institute, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, United States;4. B&B Microscopes, 490 Lowries Run Road, Pittsburgh, PA 15237, United States;5. GRECC, South Texas VA Healthcare System, San Antonio, TX 78229, United States;1. Research Institute for Earth Sciences, Geological Survey of Iran, Tehran, Iran;2. Earth Science Department, Faculty of Natural Science, University of Tabriz, Tabriz, Iran;3. Department of Petroleum Engineering, Curtin University, Perth, Western Australia, Australia;4. Department of Mining and Exploration, Faculty of Engineering, University of Tehran, Tehran, Iran;5. Department of Geophysics, Iranian Offshore Oil Company, Tehran, Iran;1. Department of Plant Physiology, Faculty of Agriculture and Economics, University of Agriculture, Pod?u?na 3, 30-239 Kraków, Poland;2. F. Górski Institute of Plant Physiology, Polish Academy of Sciences, Niezapominajek 21, 30-239 Kraków, Poland;3. Institute of Plant Production, Department of Grassland, Faculty of Agriculture and Economics, University of Agriculture, Mickiewicza 21, Kraków, Poland;4. Department of Animal Nutrition and Feed Management, Faculty of Animal Sciences, University of Agriculture, Mickiewicza 24/28, Poland;5. Department of Genetics, Faculty of Biology and Environmental Protection, University of Silesia, Jagiellonska 28, 40-032 Katowice, Poland;6. Department of Grasses, Leguminous and Energy Crops, Plant Breeding and Acclimatization Institute, Radzików, 05-870 B?onie, Poland;1. Department of Chemistry, Inorganic Chemistry Section, Jadavpur University, Kolkata 700 032, India;2. Biophysical Chemistry Laboratory, Organic and Medicinal Chemistry Division, CSIR-Indian Institute of Chemical Biology, 4, Raja S.C. Mullick Road, Kolkata 700 032, India;3. School of Chemical Sciences, National Institute of Science Education and Research, Bhubaneswar 751 005, India;4. Department of Chemistry, Tripura University, Suryamaninagar, Tripura 799 022, India;1. Department of Cell Biology and Neurosciences, Istituto Superiore di Sanità, viale Regina Elena 299, 00161 Rome, Italy;2. Department of Chemical Sciences and Technologies, University of Rome “Tor Vergata”, via della Ricerca Scientifica 1, 00133 Rome, Italy;3. Institute of Molecular Biology and Pathology, CNR - National Research Council of Italy, Department of Biochemical Sciences “A. Rossi-Fanelli”, “Sapienza” University, 00185 Rome, Italy;4. Department of Infectious Diseases, Istituto Superiore di Sanità, viale Regina Elena 299, 00161 Rome, Italy |
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| Abstract: | The most ubiquitous of the primary reactive oxygen species, formed in all aerobes, is the superoxide free radical. It is believed that the superoxide anion radical shows low reactivity and in oxidative stress it is regarded mainly as an initiator of more reactive species such as  OH and ONOO‐.In this paper, the effectiveness of inactivation of selected enzymes by radiation-generated superoxide radicals in comparison with the effectiveness of the other products of water radiolysis is examined. We investigate three enzymes: glyceraldehyde-3-phosphate dehydrogenase (GAPDH), alcohol dehydrogenase (ADH) and lactate dehydrogenase (LDH).We show that the direct contribution of the superoxide anion radical to GAPDH and ADH inactivation is significant. The effectiveness of the superoxide anion in the inactivation of GAPDH and ADG was only 2.4 and 2.8 times smaller, respectively, in comparison with hydroxyl radical. LDH was practically not inactivated by the superoxide anion.Despite the fact that the studied dehydrogenases belong to the same class of enzymes (oxidoreductases), all have a similar molecular weight and are tetramers, their susceptibility to free-radical damage varies. The differences in the radiosensitivity of the enzymes are not determined by the basic structural parameters analyzed. A significant role in inactivation susceptibility is played by the type of amino acid residues and their localization within enzyme molecules. |
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