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由镍肽复合物介导的蛋白质高度特异性氧化交联

Highly specific oxidative cross-linking of proteins mediated by a nickel-peptide complex.

作者信息

Brown K C, Yang S H, Kodadek T

机构信息

Department of Chemistry and Biochemistry, University of Texas at Austin 78712-1096, USA.

出版信息

Biochemistry. 1995 Apr 11;34(14):4733-9. doi: 10.1021/bi00014a030.

Abstract

The Ni(II) complex of the tripeptide NH2-Gly-Gly-His-COOH is shown to mediate efficient protein-protein cross-linking in the presence of oxidants such as oxone and monoperoxyphthalic acid. Only proteins that associate specifically in solution are cross-linked under these conditions. Preliminary probes of the mechanism of the reaction suggest that the active intermediate may be a high-valent metal complex that attacks aromatic amino acids.

摘要

三肽NH2-Gly-Gly-His-COOH的镍(II)配合物在过硫酸氢钾复合盐和单过氧邻苯二甲酸等氧化剂存在下可介导高效的蛋白质-蛋白质交联。在这些条件下,只有在溶液中特异性缔合的蛋白质才会发生交联。对反应机制的初步探索表明,活性中间体可能是一种攻击芳香族氨基酸的高价金属配合物。

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