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dc.contributor.authorGao, X. A.zh_CN
dc.contributor.authorHu, X. M.zh_CN
dc.contributor.authorZhu, J.zh_CN
dc.contributor.authorZeng, Z. P.zh_CN
dc.contributor.authorHan, D. X.zh_CN
dc.contributor.authorTang, G.zh_CN
dc.contributor.authorHuang, X. T.zh_CN
dc.contributor.authorXu, P. X.zh_CN
dc.contributor.authorZhao, Y. F.zh_CN
dc.contributor.author许鹏翔zh_CN
dc.date.accessioned2013-12-12T02:13:38Z
dc.date.available2013-12-12T02:13:38Z
dc.date.issued2011-04zh_CN
dc.identifier.citationJournal of the American Society For Mass Spectrometry, 2011,22(4):689-702zh_CN
dc.identifier.issn1044-0305zh_CN
dc.identifier.otherISI:000288713600010zh_CN
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/63278
dc.description.abstractCationic metal ion-coordinated N-diisopropyloxyphosphoryl dipeptides (DIPP-dipeptides) were analyzed by electrospray ionization multistage tandem mass spectrometry (ESI-MS (n) ). Two novel rearrangement reactions with hydroxyl oxygen or carbonyl oxygen migrations were observed in ESI-MS/MS of the metallic adducts of DIPP-dipeptides, but not for the corresponding protonated DIPP-dipeptides. The possible oxygen migration mechanisms were elucidated through a combination of MS/MS experiments, isotope (O-18, N-15, and H-2) labeling, accurate mass measurements, and density functional theory (DFT) calculations at the B3LYP/6-31 G(d) level. It was found that lithium and sodium cations catalyze the carbonyl oxygen migration more efficiently than does potassium and participation through a cyclic phosphoryl intermediate. In addition, dipeptides having a C-terminal hydroxyl or aromatic amino acid residue show a more favorable rearrangement through carbonyl oxygen migration, which may be due to metal cation stabilization by the donation of lone pair of the hydroxyl oxygen or aromatic pi-electrons of the C-terminal amino acid residue, respectively. It was further shown that the metal ions, namely lithium, sodium, and potassium cations, could play a novel directing role for the migration of hydroxyl or carbonyl oxygen in the gas phase. This discovery suggests that interactions between phosphorylated biomolecules and proteins might involve the assistance of metal ions to coordinate the phosphoryl oxygen and protein side chains to achieve molecular recognition.zh_CN
dc.language.isoen_USzh_CN
dc.source.urihttp://dx.doi.org/10.1007/s13361-010-0069-5zh_CN
dc.subjectCARBONYL OXYGEN MIGRATIONzh_CN
dc.subjectGAS-PHASEzh_CN
dc.subjectPROTEIN INTERACTIONSzh_CN
dc.subjectCATIONIZED PEPTIDESzh_CN
dc.subjectREARRANGEMENTzh_CN
dc.subjectDIPEPTIDESzh_CN
dc.subjectFRAGMENTATIONzh_CN
dc.subjectCOMPLEXESzh_CN
dc.subjectSPECTRAzh_CN
dc.subjectDENSITYzh_CN
dc.titleAn Isotope (O-18, N-15, and H-2) Technique to Investigate the Metal Ion Interactions Between the Phosphoryl Group and Amino Acid Side Chains by Electrospray Ionization Mass Spectrometryzh_CN
dc.typeArticlezh_CN


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