An electrochemical study of the stability of cytochrome c3 from Desulfovibrio desulfuricans Norway strain |
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| Institution: | 1. Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Jalal Al Ahmad St. P.O. Box 14115-175, Tehran, Iran;2. Center of Excellence in Electrochemistry, School of Chemistry, College of Science, University of Tehran, Tehran, Iran;3. Department of Biology, Faculty of Sciences, University of Zanjan, Zanjan, Iran;4. Department of Biology, Faculty of Sciences, University of Guilan, Rasht, Iran;5. Endocrinology & Metabolism Research Center, Tehran University of Medical Sciences, Tehran, Iran;1. Instituto de Ingeniería, Universidad Nacional Autónoma de México, México City, C.P, 04510, Mexico;2. División de Estudios de Posgrado e Investigación, ITCM, Tamaulipas, Mexico;1. University of Monastir, Laboratory of Interfaces and Advanced Materials, Faculty of Sciences, Monastir, Tunisia;2. University of Lyon, Institute of Analytical Sciences, 69100 Villeurbanne, Lyon, France;1. Center of Excellence in Electrochemistry, University of Tehran, Tehran, Iran;2. Endocrinology & Metabolism Research Center, Tehran University of Medical Sciences, Tehran, Iran;3. Iranian Research Institute of Plant Protection, Agricultural Research, Education and Extension Organization, Tehran, Iran;1. Chemistry Department, Faculty of Science at Yanbu, Taibah University, Yanbu 46423, Saudi Arabia;2. Chemistry Department, Faculty of Science, Damietta University, Damietta 34517, Egypt;3. Environmental Biotechnology Department, Genetic Engineering and Biotechnology Research Institute,University of Sadat City, Sadat City 32897, Egypt |
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| Abstract: | The electrochemical behaviour of cytochrome c3 from Desulfovibrio desulfuricans, Norway strain, remains unchanged within the pH range 5–9.5. Differential pulse polarography peaks disappear at pH < 5 and two transitions are noted at alkaline pH (10.5 and 12). In denaturation experiments, guanidinium chloride has a more marked effect than urea on differential pulse polarography and cyclic voltammetry peaks.The study of absorption spectra shows that the δ band at 351 nm of the oxidized form increases above pH ∼ 10.Neither absorption spectra nor polarograms are modified after the treatment of cytochrome c3 for 10 min at 100°C.It is concluded that hydrogen bonds must play a prominent role in maintaining the tertiary structure of the protein. Cytochrome c3 from D. desulfuricans Norway is a particularly stable molecule as regards pH, denaturing agents, temperature and ageing. |
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