How Do Enzymes Orient When Trapped on Metal-Organic Framework (MOF) Surfaces?
How Do Enzymes Orient When Trapped on Metal-Organic Framework (MOF) Surfaces?
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DOI：
10.1021/jacs.8b09257
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发表时间：
2018-11-28
影响因子：
15
通讯作者：
Yang, Zhongyu
中科院分区：
文献类型：
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作者：
Pang, Yanxiong;Li, Hui;Yang, Zhongyu
在金属有机骨架(MOF)中固定化酶可保持酶的完整性和活性，增强稳定性，并减少淋溶。在MOF表面捕获酶将允许涉及大底物的催化。在这两种情况下，催化效率和选择性不仅取决于酶的完整性/浓度，而且取决于取向。然而，确定固定在固体基质上的酶的方向一直是一个挑战，由于MOF背景信号的干扰，这对固定/捕获在MOF中的酶更具挑战性。为了应对这样的挑战，我们在这项工作中展示了结合电子顺磁共振光谱的位置定向自旋标记的使用，这首次允许表征捕获在MOF表面的酶的取向。所获得的洞察力对于基于MOF的酶固定化设计和理解一旦被捕获在固体基质甚至细胞限制条件下的酶的方向是至关重要的。
Enzyme immobilization in metal organic frameworks (MOFs) offers retained enzyme integrity and activity, enhanced stability, and reduced leaching. Trapping enzymes on MOF surfaces would allow for catalysis involving large substrates. In both cases, the catalytic efficiency and selectivity depend not only on enzyme integrity/concentration but also orientation. However, it has been a challenge to determine the orientation of enzymes that are supported on solid matrices, which is even more challenging for enzymes immobilized/trapped in MOFs due to the interferences of the MOF background signals. To address such challenge, we demonstrate in this work the utilization of site-directed spin labeling in combination with Electron Paramagnetic Resonance spectroscopy, which allows for the first time the characterization of the orientation of enzymes trapped on MOF surfaces. The obtained insights are fundamentally important for MOF-based enzyme immobilization design and understanding enzyme orientation once trapped in solid matrices or even cellular confinement conditions.