牛磺酸/α-酮戊二酸双加氧酶的Cr(II)反应活性

Cr(II) reactivity of taurine/alpha-ketoglutarate dioxygenase.

作者信息

Grzyska Piotr K, Hausinger Robert P

机构信息

Department of Microbiology & Molecular Genetics, Michigan State University, East Lansing, Michigan 48824-4320, USA.

出版信息

Inorg Chem. 2007 Nov 26;46(24):10087-92. doi: 10.1021/ic700383q. Epub 2007 Nov 1.

DOI:10.1021/ic700383q

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2596585/

Abstract

The interaction of CrII with taurine/alpha-ketoglutarate (alphaKG) dioxygenase (TauD) was examined. CrII replaces FeII and binds stoichiometrically with alphaKG to the FeII/alphaKG binding site of the protein, with additional CrII used to generate a chromophore attributed to a CrIII-semiquinone in a small percentage of the sample. Formation of the latter oxygen-sensitive species requires the dihydroxyphenylalanine (DOPA) quinone form of Tyr-73. This preformed side chain is generated by intracellular self-hydroxylation of Tyr-73 to form DOPA, which is subsequently oxidized to the quinone. No chromophore is generated when using NaBH4-treated sample, protein isolated from anaerobically grown cells, inactive TauD variants that are incapable of self-hydroxylation, or the Y73F active mutant of TauD. A CrIII-DOPA semiquinone also was observed in the herbicide hydroxylase SdpA.

摘要

研究了CrII与牛磺酸/α-酮戊二酸（αKG）双加氧酶（TauD）的相互作用。CrII取代FeII并与αKG化学计量地结合到蛋白质的FeII/αKG结合位点，在一小部分样品中额外的CrII用于生成归因于CrIII-半醌的发色团。后一种对氧敏感的物种的形成需要Tyr-73的二羟基苯丙氨酸（DOPA）醌形式。这种预先形成的侧链是由Tyr-73的细胞内自羟基化形成DOPA产生的，随后DOPA被氧化为醌。当使用NaBH4处理的样品、从厌氧生长的细胞中分离的蛋白质、不能自羟基化的无活性TauD变体或TauD的Y73F活性突变体时，不会产生发色团。在除草剂羟化酶SdpA中也观察到了CrIII-DOPA半醌。

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