Co-immobilization of an enzyme and a metal into the compartments of mesoporous silica for cooperative tandem catalysis: an artificial metalloenzyme.
Co-immobilization of an enzyme and a metal into the compartments of mesoporous silica for cooperative tandem catalysis: an artificial metalloenzyme.
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DOI：
10.1002/anie.201306487
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发表时间：
2013-12-23
影响因子：
16.6
通讯作者：
Backvall, Jan-E.
中科院分区：
文献类型：
--
作者：
Engstrom, Karin;Johnston, Eric V.;Verho, Oscar;Gustafson, Karl P. J.;Shakeri, Mozaffar;Tai, Cheuk-Wai;Backvall, Jan-E.
作为数百万年自然进化的结果，酶构成了催化领域的最新技术，它们能够在温和条件下有效催化广泛的重要化学反应。在酶中，金属酶是最令人印象深刻的例子，它们参与了自然界中的几个重要过程，如水氧化，[1]光合作用[2]和固氮。[3]在金属酶中，含金属的辅因子被整合到蛋白质结构中，以实现新的化学反应，这是单独使用蛋白质化学无法实现的。在现代社会中，酶用于化学品的大规模生产和其他工业应用的利用是公认的。[4]沿着酶的高效率，它们也是理想的可持续催化剂，因为它们是从可再生资源中获得的，并且是可生物降解的和无毒的。不幸的是，天然来源的酶的一个主要缺点是它们通常表现出狭窄的底物范围，这限制了它们在有机合成中的应用。自从Wilson和Whitesides在1978年发表了富有远见的报告以来，[5]一个长期追求的梦想就是构建具有非天然辅因子的金属酶，为新的高效催化反应开辟道路。到目前为止，已经探索了几种产生人工金属酶的方法，[6]但一般来说，它们中的大多数涉及通过共价，配位或超分子相互作用将有机金属物质锚定到蛋白质上。在这些情况中的许多情况下，金属酶的催化活性源自引入的金属物质，并且周围的蛋白质仅用作决定立体选择性的配体。近年来，高活性的多相催化剂，特别是那些基于纳米粒子的催化剂，在选择性化学转化中引起了广泛的关注。[7]已经发现，通过将簇尺寸减小到2nm以下，可以获得独特的选择性和活性。[7a]在此，我们提出了一种方法，用于构建具有两种不同反应模式的人工金属酶：一种是由纳米组分和一种酶所表现出的。通过将酶和纳米金属物质逐步固定到介孔多相载体的同一空腔中，创造了一种环境，在该环境中这些物质可以以合作的方式彼此靠近地驻留和工作。这种环境允许级联反应的简单设计，其中酶和金属催化剂可以协同串联催化。此外，这种方法将提供利用多相催化的优点的途径，具有催化剂的简单分离和再循环。开发利用生物催化和过渡金属催化潜力的催化实体的方法迄今为止仅被很少地探索。Foulkes等人改造了大肠杆菌细菌，使其同时在细胞内表达单胺氧化酶并在外膜上结合Pd纳米颗粒，然后将其用于胺去外消旋。[8]Kim及其同事最近报道了另一种有前途的生成多功能金属酶模拟物的策略，其中将Pt纳米颗粒引入氨肽酶中。[9]这种人工金属酶被成功地用于两步级联反应，包括酶催化的酰胺键断裂和Pt催化的氢化。最近，Filice等人使用相同的方法将Pd纳米颗粒引入脂肪酶的内部以获得生物杂化催化剂。[10]在我们的团队中，最近的研究...
As a result of natural evolution for millions of years, enzymes constitute the state of the art in catalysis, with their ability to efficiently catalyze a wide range of important chemical reactions under mild conditions. Among the enzymes, metalloenzymes stand out as the most impressive examples, and they are involved in several important processes in nature, such as water oxidation,[1] photosynthesis,[2] and nitrogen fixation.[3] In a metalloenzyme, a metal-containing cofactor is integrated into the protein structure to enable new chemical reactions that would not be possible to achieve with the chemistry of the protein alone. In modern society, the utilization of enzymes for large-scale production of chemicals and other industrial applications is well-established.[4] Along with the high efficiency of enzymes, they are also ideal sustainable catalysts, as they are obtained from renewable sources, and are biodegradable and non-toxic. Unfortunately, one major drawback of naturally derived enzymes is that they often exhibit a narrow substrate scope, which limits their use in organic synthesis. Ever since the visionary report by Wilson and Whitesides in 1978,[5] a longsought dream has been to construct metalloenzymes with non-natural cofactors that open up for new efficient catalytic reactions. Several approaches to generate artificial metalloenzymes have so far been explored,[6] but in general most of them involve the anchoring of an organometallic species to a protein, by either covalent, dative, or supramolecular interactions. In many of these cases the catalytic activity of the metalloenzyme originates from the introduced metal species, and the surrounding protein only serves as a ligand determining the stereoselectivty. Recently, highly active heterogeneous catalysts, and in particular those based on nanometallic species, have attracted considerable attention for selective chemical transformations.[7] It has been found that by decreasing the cluster size below 2 nm a unique selectivity and activity may be obtained.[7a] Herein, we propose an approach for the construction of an artificial metalloenzyme with two different modes of reactivity: one exhibited by a nanometallic component and one by an enzyme. By the stepwise immobilization of an enzyme and a nanometal species into the same cavity of a mesoporous heterogeneous support, an environment is created where these species can reside and work in close proximity to one another in a cooperative fashion. This environment allows a simple design of cascade reactions in which the enzyme and the metal catalyst can work in cooperative tandem catalysis. Moreover, this approach would provide access to the advantages of heterogeneous catalysis with simple separation and recycling of the catalyst. The approach of developing catalytic entities that make use of the potential of both biocatalysis and transition metal catalysis has so far only been sparingly explored. Foulkes et al. engineered Escherichia coli bacteria to simultaneously express monoamine oxidase intracellularly and bind Pd nanoparticles on the outer membrane, which were then used for amine deracemization.[8] Another promising strategy of generating multifunctional metalloenzyme mimics was recently reported by Kim and co-workers, where Pt nanoparticles were introduced into an aminopeptidase.[9] This artificial metalloenzyme was successfully employed in a twostep cascade reaction, involving enzyme-catalyzed amide bond cleavage and Pt-catalyzed hydrogenation. Very recently, the same approach was used by Filice et al. to introduce Pd nanoparticles into the interior of a lipase to obtain a biohybrid catalyst.[10]In our group, recent research has …
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影响因子：
5.2
作者：
Kwon, MS;Kim, N;Park, J
通讯作者：
Park, J
影响因子：
3.6
作者：
Gross, Elad;Krier, James M.;Somorjai, Gabor A.
通讯作者：
Somorjai, Gabor A.
影响因子：
9.9
作者：
Larsericsdotter, H;Oscarsson, S;Buijs, J
通讯作者：
Buijs, J
影响因子：
12.9
作者：
Foulkes, Joanne M.;Malone, Kirk J.;Lloyd, Jonathan R.
通讯作者：
Lloyd, Jonathan R.
影响因子：
16.6
作者：
Bos, Jeffrey;Fusetti, Fabrizia;Roelfes, Gerard
通讯作者：
Roelfes, Gerard