枯草杆菌蛋白酶与氨基环戊二烯基钌配合物作为催化剂组合对仲醇进行(S)-选择性动态动力学拆分
(S)-selective dynamic kinetic resolution of secondary alcohols by the combination of subtilisin and an aminocyclopentadienylruthenium complex as the catalysts.
作者信息
Kim Mahn-Joo, Chung Yong Il, Choi Yoon Kyung, Lee Han Ki, Kim Daeho, Park Jaiwook
机构信息
Department of Chemistry, Pohang University of Science and Technology, Pohang, Kyongbuk 790-784, Korea.
出版信息
J Am Chem Soc. 2003 Sep 24;125(38):11494-5. doi: 10.1021/ja036766r.
A new procedure for the dynamic kinetic resolution (DKR) of racemic alcohols into single enantiomers is described. This procedure employs surfactant-treated subtilisin as an (S)-selective resolving catalyst and an aminocyclopentadienylruthenium complex as a racemizing catalyst. The DKR is performed best in the presence of an acyl donor such as trifluoroethyl butyrate in THF at room temperature. Eight simple secondary alcohols have been efficiently resolved with high optical purities and good yields. The subtilisin-based DKR is complementary in stereoselectivity to its lipase-based counterpart. For an acyl-carrying alcohol, both subtilisin- and lipase-based DKRs have proceeded equally well to give a pair of enantiomeric products (>99.5% ee each) with opposite optical rotations in high yields (94-95%).
描述了一种将外消旋醇动态动力学拆分（DKR）为单一对映体的新方法。该方法使用表面活性剂处理的枯草杆菌蛋白酶作为（S）-选择性拆分催化剂，以及氨基环戊二烯基钌配合物作为消旋催化剂。在室温下于四氢呋喃中，在诸如丁酸三氟乙酯等酰基供体存在下，DKR的效果最佳。八种简单仲醇已被高效拆分，具有高光学纯度和良好产率。基于枯草杆菌蛋白酶的DKR在立体选择性上与其基于脂肪酶的对应方法互补。对于携带酰基的醇，基于枯草杆菌蛋白酶和基于脂肪酶的DKR都同样顺利地进行，以高收率（94 - 95%）得到一对具有相反旋光性的对映体产物（每种对映体的对映体过量值均>99.5%）。
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