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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
dc.contributor.author | Mozziconacci, Olivier | |
dc.contributor.author | Ji, Junyan A. | |
dc.contributor.author | Wang, Y. John | |
dc.contributor.author | Schöneich, Christian | |
dc.date.accessioned | 2017-05-09T20:57:30Z | |
dc.date.available | 2017-05-09T20:57:30Z | |
dc.date.issued | 2013-02-04 | |
dc.identifier.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 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/24059 | |
dc.description.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. | en_US |
dc.publisher | American Chemical Society | en_US |
dc.rights | This document is the Accepted Manuscript version of a Published Work that appeared in final form in Molecular Pharmaceutics, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://doi.org/10.1021/mp300563m. | en_US |
dc.subject | Parathyroid hormone | en_US |
dc.subject | Alanine | en_US |
dc.subject | Methionine | en_US |
dc.subject | Homocysteine | en_US |
dc.subject | Methionine radical cation | en_US |
dc.subject | Fenton reaction | en_US |
dc.subject | Hydrolysis | en_US |
dc.subject | Mass spectrometry | en_US |
dc.title | Metal-Catalyzed Oxidation of Protein Methionine Residues in Human Parathyroid Hormone (1-34): Formation of Homocysteine and a Novel Methionine-Dependent Hydrolysis Reaction | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Mozziconacci, Olivier | |
kusw.kuauthor | Schöneich, Christian | |
kusw.kudepartment | Pharmaceutical Chemistry | en_US |
dc.identifier.doi | 10.1021/mp300563m | en_US |
kusw.oaversion | Scholarly/refereed, author accepted manuscript | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC3691993 | en_US |
dc.rights.accessrights | openAccess |