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A Structural Mimic of Carbonic Anhydrase in a Metal-Organic Framework
Chem ( IF 23.5 ) Pub Date : 2018-10-04 , DOI: 10.1016/j.chempr.2018.09.011
Ashley M. Wright , Zhenwei Wu , Guanghui Zhang , Jenna L. Mancuso , Robert J. Comito , Robert W. Day , Christopher H. Hendon , Jeffrey T. Miller , Mircea Dincă

Metal-organic frameworks (MOFs) have exciting potential for biomimetic studies of enzymes, yet construction of high-fidelity models at the metal nodes is challenging. Nonetheless, biomimetic MOFs have significant advantages, such as increased stability and ease of separation, over their enzymatic and homogeneous counterparts, making them particularly attractive for industrial applications. Here, we demonstrate biomimetic behavior of Zn hydroxide moieties inside a MOF with structural and reactivity characteristics of carbonic anhydrase. Similar to the biological system, the MOF binds CO2 by an insertion mechanism into the Zn–OH bond, leading to significant adsorption of CO2 (3.41 mmol/g). In reactivity mimicking that of the enzyme, the material also catalyzes the oxygen isotope exchange between water and carbon dioxide. Overall, these results provide the strongest evidence yet of metal nodes in MOFs bearing high structural fidelity to enzymatic active sites.



中文翻译:

金属有机骨架中碳酸酐酶的结构模拟

金属有机框架(MOF)在酶的仿生研究方面具有令人兴奋的潜力,但是在金属节点上构建高保真模型具有挑战性。尽管如此,仿生MOF相比其酶促和均相的仿冒品具有显着的优势,例如更高的稳定性和易于分离的特性,使其对工业应用特别有吸引力。在这里,我们展示了MOF内部具有碳酸酐酶的结构和反应特性的氢氧化锌部分的仿生行为。与生物系统类似,MOF通过插入机制将CO 2结合到Zn-OH键中,从而导致CO 2的显着吸附(3.41mmol / g)。在模仿酶的反应性中,该材料还催化水和二氧化碳之间的氧同位素交换。总体而言,这些结果提供了迄今最强的证据,表明MOF中的金属节点对酶促活性位点具有很高的结构保真度。

更新日期:2018-10-04
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