Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208-3113, United States.
Department of Materials Science and Engineering, Northwestern University, Evanston, Illinois 60208, United States.
J Am Chem Soc. 2020 Oct 28;142(43):18576-18582. doi: 10.1021/jacs.0c07870. Epub 2020 Oct 13.
The encapsulation of enzymes within porous materials has shown great promise, not only in protecting the enzymes from denaturation under nonbiological environments, but also, in some cases, in facilitating their enzymatic reaction rates at favorable reaction conditions. While a number of hypotheses have been developed to explain this phenomenon, the detailed structural changes of the enzymes upon encapsulation within the porous material, which are closely related to their activity, remain largely elusive. Herein, the structural change of cytochrome c (Cyt c) upon encapsulation within a hierarchical metal-organic framework, NU-1000, is investigated through a combination of experimental and computational methods, such as electron paramagnetic resonance, solid-state ultraviolet-visible spectroscopy, and all-atom explicit solvent molecular dynamics simulations. The enhanced catalytic performance of Cyt c after being encapsulated within NU-1000 is supported by the physical and in silico observations of a change around the heme ferric active center.
将酶封装在多孔材料中显示出巨大的潜力，不仅可以在非生物环境中防止酶变性，而且在某些情况下还可以在有利的反应条件下促进其酶反应速率。虽然已经提出了许多假设来解释这种现象，但与酶活性密切相关的酶在多孔材料中封装时的详细结构变化在很大程度上仍难以捉摸。在此，通过电子顺磁共振、固态紫外-可见光谱和全原子显式溶剂分子动力学模拟等实验和计算方法，研究了细胞色素 c（Cyt c）在分级金属-有机骨架 NU-1000 中封装时的结构变化。在 NU-1000 中封装后 Cyt c 的增强催化性能得到了围绕血红素铁活性中心的物理和计算机观察的支持。
