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    J Am Chem Soc. 2011 Oct 12;133(40):15803-5. Epub 2011 Sep 19.

    The biological buffer bicarbonate/CO2 potentiates H2O2-mediated inactivation of protein tyrosine phosphatases.

    Zhou H, Singh H, Parsons ZD, Lewis SM, Bhattacharya S, Seiner DR, LaButti JN, Reilly TJ, Tanner JJ, Gates KS.

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    Department of Chemistry, University of Missouri, Columbia, Missouri 65211, United States.

    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).

    PMID:
    21913686
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC3268130
    [Available on 2012/10/12]

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