Size-selective olefin hydrogenation by a Pd nanocluster provided in an apo-ferritin cage
Size-selective olefin hydrogenation by a Pd nanocluster provided in an apo-ferritin cage
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DOI：
10.1002/anie.200353436
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发表时间：
2004-01-01
影响因子：
16.6
通讯作者：
Watanabe, Y
中科院分区：
文献类型：
--
作者：
Ueno, T;Suzuki, M;Watanabe, Y
There has been much interest lately in chemical transformations in single capsules of supramolecular assemblies.[1–4] Well-designed capsule structures could provide increased concentration of substrates in the cavities with high selectivity to allow transformation of the substrates. Proteins are very attractive building components for the construction of selfassembled cage structures.[1, 5–12] For example, Mann and coworkers have reported in their pioneering works the preparation of size-restricted metal oxides and sulfides by using the biosupramolecular cage of ferritin.[5–7] In addition, protein assemblies of viruses and the chaperonin protein GroEL were also utilized for the encapsulation of metal nanoclusters.[10–12] However, difficulties still remain in controlling reactions catalyzed by metal clusters in protein cages. Ferritin is known as an iron-storage protein and comprises 24 subunits that assemble to form a hollow cagelike structure of 12 nm in diameter as shown in Figure 1. Iron atoms are stored as a cluster of ferric oxyhydroxide within a cavity of diameter 8 nm formed by the protein subunits (Figure 1 b).[13, 14] One of the most important consequences of this protein cage is the perforation of the protein shell by small channels that locate at the junctions of the subunits (Figure 1 c and d). The channels are required for the transport of several metal ions and other organic molecules.[15] In addition, penetration studies of organic molecules have
