Generation of hydrogen peroxide by incidental metal ion-catalyzed autooxidation of glutathione |
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| Authors: | P W Albro J T Corbett J L Schroeder |
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| Institution: | 1. Department of Chemistry, Capital Normal University, Beijing 100048, China;2. The College of Materials Science and Engineering, Beijing University of Technology, Beijing 100022, China;3. School of Science , Minzu University of China, Beijing 100081, China;4. School of Food and Chemical Engineering, Beijing Technology and Business University, Beijing 100048, China;1. Materials Science Laboratory, Department of Physics, Periyar University, Salem, Tamil Nadu, 636011, India;2. Department of Physics, ERK College of Arts and Science, Dharmapuri, Tamil Nadu, 636905, India;1. Inorganic & Nanomaterials Research Laboratory, Department of Chemistry, Bharathiar University, Coimbatore 641 046, India;2. Department of Chemistry, University of Washington, Seattle, WA 98195, USA;1. Department of Agronomy and Plant Breeding Sciences, College of Aburaihan, University of Tehran, Tehran, Iran;2. Department of Plant Biotechnology, Faculty of Life Science and Biotechnology, Shahid Beheshti University, G.C. Tehran, Iran;3. Department of Plant Genetics and Breeding, Faculty of Agriculture, Tarbiat Modares University, Tehran, Iran;4. Dipartimento di Agraria, Università di Napoli Federico II, Portici, NA, Italy |
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| Abstract: | Autooxidation of reduced glutathione in 50 mM buffer at pH 7.9 is indetectably slow in the presence of 1 mM DETAPAC, EDTA, TET, or tripyridine, but passing buffer through Chelex resin was insufficient to remove traces of catalytically active metals. Production of hydrogen peroxide during glutathione autooxidation was catalyzed by traces of Fe+2 or Cu+2, and to a much lesser extent by Cu+1 and Ni+2, but not to a detectable extent by Na+1, K+1, Fe+3, Al+3, Cd+2, Zn+2, Ca+2, Mg+2, Mn+2, or Hg+2. Cysteine was a much better precursor for hydrogen peroxide production than were cysteine sulfinic or sulfonic acids. The chelators EGTA, NTA, bipyridine, dimethyl glyoxime, salicylate, and Desferal were ineffective at preventing autooxidation. EDDA and 8-hydroxyquinoline were partially effective. Catalase could completely prevent the accumulation of detectable H2O2, but superoxide dismutase was only slightly inhibitory. Hydroxyl radical and singlet oxygen quenching agents (mannitol and histidine) stimulated. A mechanism for the production of H2O2 during trace metal catalyzed oxidation of glutathione is proposed, involving glutathione-complexed metal and dissolved oxygen. Although a radical intermediate can not be ruled out, no radical initiated chain reaction is necessary. |
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