Electrochemical nitration of myoglobin at tyrosine 103: Structure and stability

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Title: Electrochemical nitration of myoglobin at tyrosine 103: Structure and stability
Authors: Gomez-Mingot, Maria | Alcaraz Mas, Luis Antonio | Heptinstall, John | Donaire González, Antonio | Piccioli, Mario | Montiel, Vicente | Iniesta, Jesus
Research Group/s: Electroquímica Aplicada y Electrocatálisis
Center, Department or Service: Universidad de Alicante. Departamento de Química Física | Universidad de Alicante. Instituto Universitario de Electroquímica
Keywords: Oxidative stress | Electronitration | 3-Nitro-tyrosine | Heme myoglobin | Boron doped diamond | NMR
Knowledge Area: Química Física
Issue Date: 1-Jan-2013
Publisher: Elsevier
Citation: Archives of Biochemistry and Biophysics. 2013, 529(1): 26-33. doi:10.1016/j.abb.2012.10.013
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.
Sponsor: Financial support from the Ministerio de Educación y Ciencia MEC Spain (project CTQ2007-62345), (project CTQ2010-18570) and EUNMR project (Contract #RII3-026145) is gratefully acknowledged.
URI: http://hdl.handle.net/10045/38719
ISSN: 0003-9861 (Print) | 1096-0384 (Online)
DOI: 10.1016/j.abb.2012.10.013
Language: eng
Type: info:eu-repo/semantics/article
Peer Review: si
Publisher version: http://dx.doi.org/10.1016/j.abb.2012.10.013
Appears in Collections:INV - LEQA - Artículos de Revistas
INV - BIOTECEXTREM - Artículos de Revistas

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