کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
219172 | 463251 | 2013 | 7 صفحه PDF | دانلود رایگان |
Protein phosphorylation by kinases plays a significant role in a wide range of cellular processes. Phosphotyrosine is the product of tyrosine phosphorylation. The electrochemical behaviour of phosphotyrosine (pTyr) at a glassy carbon electrode was investigated over a wide pH range, using cyclic, differential pulse and square-wave voltammetry. The oxidation is an irreversible, pH-independent process that involves the transfer of one electron and no proton. The oxidation of phosphotyrosine occurs in a cascade mechanism and for acid electrolytes one electroactive product was observed. In neutral and alkaline electrolytes two redox products that undergo reversible, pH-dependent redox reactions with the transfer of two electrons and two protons were characterised. Also, the oxidation of tyrosine was studied in order to find information about the redox products of phosphotyrosine. A redox mechanism for phosphotyrosine was proposed. The present study provides information concerning an electroanalytical signal for studying protein phosphorylation processes.
Chemical structure of phosphotyrosine and DP voltammograms recorded in 100 μM phosphotyrosine in pH = 7.0 0.1 M phosphate buffer: (···) first and (–) second scans.Figure optionsDownload as PowerPoint slideHighlights
► The electrochemical behaviour of phosphotyrosine was studied over a wide pH range.
► The oxidation of phosphotyrosine is irreversible and pH-independent.
► For acid electrolytes one electroactive product was characterised.
► In neutral and alkaline electrolytes two redox products were observed.
► A redox mechanism for the oxidation of phosphotyrosine was proposed.
Journal: Journal of Electroanalytical Chemistry - Volume 689, 15 January 2013, Pages 216–222