Electrochemical nitration of myoglobin at tyrosine 103: Structure and stability |
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| Authors: | Maria Gómez-Mingot Luis A Alcaraz John Heptinstall Antonio Donaire Mario Piccioli Vicente Montiel Jesús Iniesta |
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| Institution: | 1. Physical Chemistry Department and Institute of Electrochemistry, University of Alicante, 03690 San Vicente del Raspeig, Alicante, Spain;2. Centre for Molecular and Biomedical Science, Faculty of Health and Life Sciences, Coventry University, Coventry CV1 5FB, UK;3. Department of Inorganic Chemistry, University of Murcia, Campus Universitario de Espinardo, 30100 Espinardo, Murcia, Spain;4. Magnetic Resonance Centre (CERM), Via Luigi Sacconi, 6, Polo Scientifico University of Florence, 50019 Sesto Florentino, Italy;1. Fluoro Organic Division, Indian Institute of Chemical Technology, Hyderabad 500 607, India;2. Biology Division, Indian Institute of Chemical Technology, Tarnaka, Hyderabad 500 607, India;1. Acoris Research (A Division of Hikal Ltd), 3A, International Biotech Park, Hinjewadi, Pune 411 057, Maharashtra, India;2. Hikal R&D Centre, No. 32/1, Kalena Agrahara, Bannerghatta Road, Bangalore 560 076, Karnataka, India;1. Department of Chemistry, 260 Science and Engineering Building, Oakland University, Rochester, MI 48309-4477, USA;2. School of Chemistry, The University of Edinburgh, Edinburgh EH9 3JJ, UK;1. Institute of Chemistry, The Hebrew University, Edmond Safra Campus, Givat Ram, 91904 Jerusalem, Israel;2. Dipartimento di Chimica, Universita di Perugia, Via Elce di Sotto, 8, Perugia, Italy;1. Department of Orthodontics, New York University College of Dentistry, 345 E 24th St, New York, NY 10010;2. Department of Epidemiology and Health Promotion, New York University College of Dentistry, New York, NY;3. New York University College of Dentistry, New York, NY;4. Consortium for Translational Orthodontic Research, New York University College of Dentistry, New York, NY;5. Department of Developmental Biology, Harvard School of Dental Medicine, Boston, MA;1. Department of Materials Science and Engineering, Yonsei University, 50 Yonsei-ro, Seo-dae-mun-gu, Seoul 120-749, Republic of Korea;2. Institute of Pharmaceutical and Medical Chemistry, University of Muenster, Muenster, Germany;3. College of Life Science and Bioengineering, Incheon National University, Incheon, Republic of Korea;4. Korea Institute of Science and Technology (KIST), Seoul, Republic of Korea |
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| Abstract: | Nitration in proteins is a physiologically relevant process and the formation of 3-nitrotyrosine was first proposed as an in vivo marker of the production of reactive nitrogen species in oxidative stress. No studies have been published on structural changes associated with nitration of myoglobin. To address this deficiency the electrochemical nitration of equine skeletal muscle (Mb) at amino acid tyrosine 103 has been investigated for the evaluation and characterization of structural and thermal stability changes. Y103 in Mb is one of the most exposed tyrosine residues and it is also close to the heme group. Effects of Y103 nitration on the secondary and tertiary structure of Y103 have been studied by UV–Vis, circular dichroism, fluorescence and NMR spectroscopy and by electrochemical studies. At physiological pH, subtle changes were observed involving slight loosening of the tertiary structure and conformational exchange processes. Thermal stability of the nitrated protein was found to be reduced by 5 °C for the nitrated Mb compared with the native Mb at physiological pH. Altogether, NMR data indicates that nitrated Mb has a very similar tertiary structure to that of native Mb, although with a slightly open conformation. |
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