Spectroscopic analyses of 2-oxoglutarate-dependent oxygenases: TauD as a case study.
Spectroscopic analyses of 2-oxoglutarate-dependent oxygenases: TauD as a case study.
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DOI：
10.1007/s00775-016-1406-3
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发表时间：
2017-04
期刊：
影响因子：
--
通讯作者：
Hausinger RP
中科院分区：
文献类型：
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作者：
Proshlyakov DA;McCracken J;Hausinger RP
广泛的光谱方法已被用来询问2-酮戊二酸（2 OG）依赖性加氧酶的单核铁转运中心。从这些光谱研究的结果提供了宝贵的见解，在底物结合和催化过程中的活性位点的结构变化，从而提供了重要的信息，补充这些酶的X射线晶体学，生物化学和计算方法的调查。这个迷你审查突出牛磺酸羟化酶（牛磺酸：2 OG双加氧酶，TauD）作为一个案例研究，以说明丰富的知识，可以通过应用各种各样的光谱调查产生一个单一的酶。特别是，电子吸收，圆二色性，磁性圆二色性，传统的和脉冲电子顺磁，穆斯堡尔，X射线吸收，和共振拉曼方法已被利用，以揭示在Tau D的金属网站的属性。
A wide range of spectroscopic approaches have been used to interrogate the mononuclear iron metallocenter in 2-oxoglutarate (2OG)-dependent oxygenases. The results from these spectroscopic studies have provided valuable insights into the structural changes at the active site during substrate binding and catalysis, thus providing critical information that complements investigations of these enzymes by x-ray crystallography, biochemical, and computational approaches. This mini-review highlights taurine hydroxylase (taurine:2OG dioxygenase, TauD) as a case study to illustrate the wealth of knowledge that can be generated by applying a diverse array of spectroscopic investigations to a single enzyme. In particular, electronic absorption, circular dichroism, magnetic circular dichroism, conventional and pulse electron paramagnetic, Mössbauer, X-ray absorption, and resonance Raman methods have been exploited to uncover the properties of the metal site in TauD.