X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase
X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase
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DOI：
10.1038/nsb824
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发表时间：
2002-08-01
期刊：
影响因子：
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通讯作者：
Yamaguchi, H
中科院分区：
文献类型：
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作者：
Kim, M;Okajima, T;Yamaguchi, H
铜胺氧化酶中的醌辅因子TPQ是通过活性位点酪氨酸残基的翻译后修饰产生的。利用X射线晶体学方法，我们研究了铜离子对球形节杆菌TPQ的自氧化过程的影响。载脂蛋白酶晶体厌氧浸泡与铜，从这个晶体确定的结构提供了一个视图的初始状态：未修饰的酪氨酸配位结合铜。暴露的铜绑定晶体的氧气导致形成的冷冻捕获的中间体，结构分析表明，这些中间体含有二羟基苯丙氨酸醌和三羟基苯丙氨酸。这些是铜胺氧化酶中TPQ生物合成过程中第一个可视化的中间体。
The quinone cofactor TPQ in copper amine oxidase is generated by posttranslational modification of an active site tyrosine residue. Using X-ray crystallography, we have probed the copper-dependent autooxidation process of TPQ in the enzyme from Arthrobacter globiformis. Apo enzyme crystals were anaerobically soaked with copper; the structure determined from this crystal provides a view of the initial state: the unmodified tyrosine coordinated to the bound copper. Exposure of the copper-bound crystals to oxygen led to the formation of freeze-trapped intermediates; structural analyses indicate that these intermediates contain dihydroxyphenylalanine quinone and trihydroxyphenylalanine. These are the first visualized intermediates during TPQ biogenesis in copper amine oxidase.