State Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing 100029, China.
Beijing Advanced Innovation Center for Soft Matter Science and Engineering, Beijing University of Chemical Technology, Beijing 100029, China.
ACS Synth Biol. 2024 Apr 19;13(4):1100-1104. doi: 10.1021/acssynbio.4c00123. Epub 2024 Apr 8.
A proline-based artificial enzyme is prepared by grafting the l-proline moieties onto the surface of bovine serum albumin (BSA) protein through atom transfer radical polymerization (ATRP). The artificial enzyme, the BSA-PolyProline conjugate, prefers to catalyze the formation of unsaturated ketones rather than β-hydroxy ketones in the reaction between acetone and aldehydes, which is difficult to achieve in free-proline catalysis. The altered reaction selectivity is ascribed to the locally concentrated l-proline moieties surrounding the BSA molecule, indicating a microenvironmental effect-induced switching of the reaction mechanism. Taking advantage of this selectivity, we used this artificial enzyme in conjunction with a natural enzyme, old yellow enzyme 1 (OYE1), to demonstrate a simple synthesis of different aliphatic ketones from acetone and aldehydes via tandem catalysis.
通过原子转移自由基聚合（ATRP），将 l-脯氨酸片段接枝到牛血清白蛋白（BSA）蛋白表面，制备了一种基于脯氨酸的人工酶。人工酶，即 BSA-聚脯氨酸缀合物，在丙酮与醛之间的反应中更倾向于催化不饱和酮的形成，而不是β-羟基酮，这在游离脯氨酸催化中很难实现。这种改变的反应选择性归因于围绕 BSA 分子的局部浓缩的 l-脯氨酸片段，表明反应机制的微环境效应诱导转换。利用这种选择性，我们将这种人工酶与天然酶——老黄酶 1（OYE1）结合使用，通过串联催化，从丙酮和醛合成了不同的脂肪族酮。
