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由工程化蛋白质容器构建的独立式金属氧化物纳米颗粒超晶格展现出晶内催化活性。

Free-Standing Metal Oxide Nanoparticle Superlattices Constructed with Engineered Protein Containers Show in Crystallo Catalytic Activity.

作者信息

Lach Marcel, Künzle Matthias, Beck Tobias

机构信息

RWTH Aachen University, Institute of Inorganic Chemistry; JARA-SOFT (Researching Soft Matter); and I3TM, 52074, Aachen, Germany.

出版信息

Chemistry. 2017 Dec 11;23(69):17482-17486. doi: 10.1002/chem.201705061. Epub 2017 Nov 24.

DOI:10.1002/chem.201705061
PMID:29076566
Abstract

The construction of defined nanostructured catalysts is challenging. In previous work, we established a strategy to assemble binary nanoparticle superlattices with oppositely charged protein containers as building blocks. Here, we show that these free-standing nanoparticle superlattices are catalytically active. The metal oxide nanoparticles inside the protein scaffold are accessible for a range of substrates and show oxidase-like and peroxidase-like activity. The stable superlattices can be reused for several reaction cycles. In contrast to bulk nanoparticle-based catalysts, which are prone to aggregation and difficult to characterize, nanoparticle superlattices based on engineered protein containers provide an innovative synthetic route to structurally defined heterogeneous catalysts with control over nanoparticle size and composition.

摘要

构建特定的纳米结构催化剂具有挑战性。在之前的工作中,我们建立了一种策略,以带相反电荷的蛋白质容器作为构建单元来组装二元纳米颗粒超晶格。在此,我们表明这些独立的纳米颗粒超晶格具有催化活性。蛋白质支架内的金属氧化物纳米颗粒可与多种底物接触,并表现出类似氧化酶和过氧化物酶的活性。这种稳定的超晶格可重复用于多个反应循环。与容易聚集且难以表征的块状纳米颗粒基催化剂不同,基于工程化蛋白质容器的纳米颗粒超晶格提供了一种创新的合成途径,可用于构建结构明确的多相催化剂,并能控制纳米颗粒的尺寸和组成。

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