Rapid Nitrogen Inversion Pathway in the cis/trans Isomerization of Selenoxo Peptide Bonds

Authors

  • Yun Huang,

    1. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale (Germany), Fax: (+49) 345-5511972
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  • Dr. Günther Jahreis,

    1. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale (Germany), Fax: (+49) 345-5511972
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  • Dr. Christian Lücke,

    1. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale (Germany), Fax: (+49) 345-5511972
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  • Prof. Gunter Fischer

    Corresponding author
    1. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale (Germany), Fax: (+49) 345-5511972
    • Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale (Germany), Fax: (+49) 345-5511972
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Abstract

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Two sides to a nitrogen: The cis to trans isomerization of selenoxo peptides in alkaline conditions is rationalized in terms of rapid nitrogen inversion of the tautomeric selenoimidate anion [C(Se)[DOUBLE BOND]N[BOND]] (see scheme), which increases the isomerization rate by about 30-fold as compared to the rotational pathway of the [CSe[BOND]NH[BOND]] form. The current work identifies the imino tautomer of a selenoxo peptide bond as a potential means to enhance oligopeptide backbone dynamics in a site-specific manner.

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