The co-oxidation of ammonia to nitrite during the aerobic xanthine oxidase reaction |
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| Authors: | T Nagano I Fridovich |
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| Affiliation: | 1. BHF Centre of Research Excellence, Division of Cardiovascular Medicine, Radcliffe Department of Medicine, John Radcliffe Hospital, University of Oxford, Oxford OX3 9DU, United Kingdom;2. Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7FZ, United Kingdom;3. Oxford Parkinson''s Disease Centre, Department of Physiology, Anatomy and Genetics, South Parks Road, Oxford OX1 3QX, United Kingdom;4. Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QR, United Kingdom;1. Tianjin Key Laboratory for Modern Drug Delivery & High-Efficiency, Collaborative Innovation Center of Chemical Science and Engineering, School of Pharmaceutical Science and Technology, Tianjin University, Tianjin 300072, China;2. Frontiers Science Center for Synthetic Biology (Ministry of Education), Tianjin University, Tianjin 300072, China;3. Key Laboratory of Systems Bioengineering (Ministry of Education), School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China;4. Department of Chemistry, Tianjin University, Tianjin 300072, P.R. China;5. Singapore Institute of Food and Biotechnology Innovation, Agency for Science, Technology and Research (A1STAR), Singapore 138669, Singapore;6. Tianjin Key Laboratory of Radiation Medicine and Molecular Nuclear Medicine, Institute of Radiation Medicine, Chinese Academy of Medical Sciences & Peking Union Medical College, Tianjin 300192, P.R. China;7. Tianjin Speerise Challenge Biotechnology Co., Ltd., Zhangjiawo Industrial Park, No. 16 Huiyuan Road, Zhangjiawo Town, Xiqing District, Tianjin 300380, China;8. Meining Pharma Inc, 2-401-1, Bldg 8, Huiying Industrial Park, No. 86 West Zhonghuan Road, Tianjin Pilot Free Trade Zone, Tianjin 300308, China;9. Department of Hematology, West China Hospital, Sichuan University, Chengdu 610041, China |
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| Abstract: | The xanthine oxidase reaction causes a co-oxidation of NH3 to NO2-, which was inhibitable by superoxide dismutase, catalase, hydroxyl radical scavengers, or by the chelating agents, desferrioxamine or diethylene triaminepentaacetic acid. Hydroxylamine was oxidized to NO2- much more rapidly than was NH3, and in this case superoxide dismutase or the chelating agents inhibited but catalase or the HO. scavengers did not. Hydrazine was not detectably oxidized to NO2-, and NO2- was not oxidized to NO3-, by the xanthine oxidase reaction. These results are accommodated by a reaction scheme involving (a) the metal-catalyzed production of HO. from O2- + H2O2; (b) the oxidation of H3N to H2N. by OH.; (c) the coupling of H2N. with O2- to yield peroxylamine, which hydrolyzes to hydroxylamine plus H2O2; (d) the metal-catalyzed oxidation of HO-NH2 to (Formula: see text), which couples with O2- to yield (Formula: see text), which finally dehydrates to yield NO2-. |
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