Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl μ-sulfide ligand in the binuclear manganese cluster
Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl μ-sulfide ligand in the binuclear manganese cluster
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DOI：
10.1021/ja071567j
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发表时间：
2007-05-23
影响因子：
15
通讯作者：
Christianson, David W.
中科院分区：
文献类型：
--
作者：
Di Costanzo, Luigi;Pique, Michael E.;Christianson, David W.
人类精氨酸酶i -硫代氨基脲配合物的晶体结构揭示了双核锰簇中不寻常的硫羰基多硫化物配体。巯基氨基脲的CS部分桥接Mn-A（2+）和Mn-B(2+)，配位距离分别为2.6和2.4 A。否则，巯基氨基脲与人精氨酸酶I的结合不会引起活性位点的任何显著结构变化。无配体酶的晶体结构揭示了一个氢键水分子，它可以支持质子在水分子和H141之间转移，从而在催化的最后一步再生亲核的氢氧离子。
The crystal structure of the human arginase I-thiosemicarbazide complex reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster. The CS moiety of thiosemicarbazide bridges Mn-A(2+) and Mn-B(2+) with coordination distances of 2.6 and 2.4 A, respectively.Otherwise, the binding of thiosemicarbazide to human arginase I does not cause any significant structural changes in the active site. The crystal structure of the unliganded enzyme reveals a hydrogen-bonded water molecule that could support proton transfer between a mu-water molecule and H141 to regenerate the nucleophilic mu-hydroxide ion in the final step of catalysis.