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Metal-Catalyzed Oxidation of Protein Methionine Residues in Human Parathyroid Hormone (1-34): Formation of Homocysteine and a Novel Methionine-Dependent Hydrolysis Reaction
Mozziconacci, Olivier Ji, Junyan A. Wang, Y. John Schöneich, Christian
Mozziconacci, Olivier
Ji, Junyan A.
Wang, Y. John
Schöneich, Christian
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Abstract
The oxidation of PTH(1-34) catalyzed by ferrous ethylenediaminetetraacetic acid (EDTA) is site-specific. The oxidation of PTH(1-34) is localized primarily to the residues Met[8] and His[9]. Beyond the transformation of Met[8] and His[9] into methionine sulfoxide and 2-oxo-histidine, respectively, we observed a hydrolytic cleavage between Met[8] and His[9]. This hydrolysis requires the presence of FeII and oxygen and can be prevented by diethylenetriaminepentaacetic acid (DTPA) and phosphate buffer. Conditions leading to this site-specific hydrolysis also promote the transformation of Met[8] into homocysteine, indicating that the hydrolysis and transformation of homocysteine may proceed through a common intermediate.
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2013-02-04
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American Chemical Society
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Mozziconacci_2013.pdf
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Parathyroid hormone, Alanine, Methionine, Homocysteine, Methionine radical cation, Fenton reaction, Hydrolysis, Mass spectrometry
Citation
Mozziconacci, O., Ji, J. A., Wang, Y. J., & Schöneich, C. (2013). Metal-Catalyzed Oxidation of Protein Methionine Residues in Human Parathyroid Hormone (1-34): Formation of Homocysteine and a Novel Methionine-Dependent Hydrolysis Reaction. Molecular Pharmaceutics, 10(2), 739–755. http://doi.org/10.1021/mp300563m