A structural and functional model for the 1-aminocyclopropane-1-carboxylic acid oxidase.
A structural and functional model for the 1-aminocyclopropane-1-carboxylic acid oxidase.
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DOI：
10.1002/anie.201502529
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发表时间：
2015-10
影响因子：
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通讯作者：
M. Sallmann;F. Oldenburg;B. Braun;M. Réglier;A. Simaan;C. Limberg
中科院分区：
文献类型：
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作者：
M. Sallmann;F. Oldenburg;B. Braun;M. Réglier;A. Simaan;C. Limberg
报道了迄今为止最逼真的1-氨基环丙烷-1-羧酸氧化酶(ACCO)的低分子类似物。ACCOS2-His-1-羧酸铁(II)活性中心被天然底物ACC可以与之结合的TPFE部分模拟。根据对镍类似物进行的X射线衍射分析，得到的络合物[Tp(Me，Ph)FeACC](1)代表了一个很好的结构模型，具有ACC以双齿方式配位的特征-如酶底物络合物所建议的那样-以及形成第一个成功复制ACCO功能的基础的空白配位：1是第一个已知的与O2反应生成乙烯的ACC络合物。由于FeOOH物种被认为是催化循环中的中间体，所以也测试了H_2O_2作为氧化剂，事实上，乙烯的释放甚至更快，产生了65%的产率。
The hitherto most realistic low-molecular-weight analogue for the 1-aminocyclopropane-1-carboxylic acid oxidase (ACCO) is reported. The ACCOs 2-His-1-carboxylate iron(II) active site was mimicked by a TpFe moiety, to which the natural substrate ACC could be bound. The resulting complex [Tp(Me,Ph) FeACC] (1), according to X-ray diffraction analysis performed for the nickel analogue, represents an excellent structural model, featuring ACC coordinated in a bidentate fashion-as proposed for the enzymatic substrate complex-as well as a vacant coordination site that forms the basis for the first successful replication also of the ACCO function: 1 is the first known ACC complex that reacts with O2 to produce ethylene. As a FeOOH species had been suggested as intermediate in the catalytic cycle, H2 O2 was tested as the oxidant, too, and indeed evolution of ethylene proceeded even more rapidly to give 65 % yield.