The biological buffer bicarbonate/CO2 potentiates H2O2-mediated inactivation of protein tyrosine phosphatases |
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Authors: | Zhou Haiying Singh Harkewal Parsons Zachary D Lewis Sarah M Bhattacharya Sanjib Seiner Derrick R LaButti Jason N Reilly Thomas J Tanner John J Gates Kent S |
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Institution: | Department of Chemistry, University of Missouri, Columbia, Missouri 65211, United States. |
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Abstract: | Hydrogen peroxide is a cell signaling agent that inactivates protein tyrosine phosphatases (PTPs) via oxidation of their catalytic cysteine residue. PTPs are inactivated rapidly during H(2)O(2)-mediated cellular signal transduction processes, but, paradoxically, hydrogen peroxide is a rather sluggish PTP inactivator in vitro. Here we present evidence that the biological buffer bicarbonate/CO(2) potentiates the ability of H(2)O(2) to inactivate PTPs. The results of biochemical experiments and high-resolution crystallographic analysis are consistent with a mechanism involving oxidation of the catalytic cysteine residue by peroxymonocarbonate generated via the reaction of H(2)O(2) with HCO(3)(-)/CO(2). |
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