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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols.
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Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols.

机译：邻苯三酚-间苯三酚反羟化酶的晶体结构，一种能够在分子之间进行分子间羟基转移的Mo酶。

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摘要

The Mo enzyme transhydroxylase from the anaerobic microorganism Pelobacter acidigallici catalyzes the conversion of pyrogallol to phloroglucinol. Such trihydroxybenzenes and their derivatives represent important building blocks of plant polymers. None of the transferred hydroxyl groups originates from water during transhydroxylation; instead a cosubstrate, such as 1,2,3,5-tetrahydroxybenzene, is used in a reaction without apparent electron transfer. Here, we report on the crystal structure of the enzyme in the reduced Mo(IV) state, which we solved by single anomalous-diffraction technique. It represents the largest structure (1,149 amino acid residues per molecule, 12 independent molecules per unit cell), which has been solved so far by single anomalous-diffraction technique. Tranhydroxylase is a heterodimer, with the active Mo-molybdopterin guanine dinucleotide (MGD)(2) site in the alpha-subunit, and three [4Fe-4S] centers in the beta-subunit. The latter subunit carries a seven-stranded, mainly antiparallel beta-barrel domain. We propose a scheme for the transhydroxylation reaction based on 3D structures of complexes of the enzyme with various polyphenols serving either as substrate or inhibitor.
机译：来自厌氧微生物丙酸伯劳氏菌的Mo酶转羟化酶可催化邻苯三酚转化为间苯三酚。此类三羟基苯及其衍生物是植物聚合物的重要组成部分。在转移羟基化过程中，转移的羟基均不来自水；而是在没有明显电子转移的反应中使用共底物，例如1,2,3,5-四羟基苯。在这里，我们报告在还原的Mo（IV）状态下的酶的晶体结构，这是我们通过单一异常衍射技术解决的。它代表了最大的结构（每个分子1,149个氨基酸残基，每个单位细胞12个独立分子），到目前为止，已经通过单一异常衍射技术解决了该结构。 Tranhydroxylase是一种异二聚体，在α亚基中具有活性Mo-钼蝶呤鸟嘌呤二核苷酸（MGD）（2）位点，在β亚基中具有三个[4Fe-4S]中心。后者的亚基带有一个七链，主要是反平行的β-桶状结构域。我们提出了一种基于酶与各种多酚作为底物或抑制剂的复合物的3D结构进行羟基转移反应的方案。

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