An Artificial Oxygenase Built from Scratch: Substrate Binding Site Identified Using a Docking Approach
An Artificial Oxygenase Built from Scratch: Substrate Binding Site Identified Using a Docking Approach
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DOI：
10.1002/anie.201209021
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发表时间：
2013-01-01
影响因子：
16.6
通讯作者：
Menage, Stephane
中科院分区：
文献类型：
--
作者：
Esmieu, Charlene;Cherrier, Mickael V.;Menage, Stephane
对可持续化学的需求促使科学界设计清洁的化学工艺。在这种背景下，绿色化学的概念已经出现，[1]涉及避免使用和产生有害物质的十二项原则。生物催化是一种很有前途的策略，它满足了大多数这些原则（催化，有机溶剂的还原，无危险的合成和选择性反应，原子经济性，无毒金属等）。[2]为特定反应创造新的生物催化剂的一种方法是设计人工金属酶，其基于基于金属基催化（通过无机络合物）和蛋白质驱动的反应选择性的组合，从而赋予生物分子非天然活性。[3]与天然酶相比，这些杂合体的优点在于基于嵌入蛋白质内的无机复合物的结构修饰的额外优化程度。已经使用人工金属酶处理了各种各样的反应。[5]其中，氧化领域似乎是有前途的，因为人工杂交体可以克服双（单）加氧酶的缺点，也就是说，需要多蛋白复合物，包括氧化还原伴侣（例如铁氧化还原蛋白或NADPH还原酶）。[6]美国
The need for sustainable chemistry urges the scientific community to design clean chemical processes. In this context, the concept of green chemistry has emerged,[1] and involves twelve principles with respect to avoiding both the use and the generation of hazardous substances. Biocatalysis is a promising strategy which fulfills most of these principles (catalysis, reduction of organic solvent, nondangerous synthesis and selective reactions, atom economy, nontoxic metals, etc.).[2] One approach to creating new biocatalysts for a defined reaction is the design of artificial metalloenzymes which are based on the combination of metal-based catalysis (by an inorganic complex) and protein-driven reaction selectivity, thus conferring unnatural activities to biomolecules.[3] Compared to natural enzymes, the advantage of these hybrids resides in an additional degree of optimization based on structural modifications of the inorganic complex embedded within the protein. A great variety of reactions has been tackled using artificial metalloenzymes.[5] Among them, the field of oxidation seems to be promising because artificial hybrids can overcome the drawbacks of di (mono) oxygenases, that is, the requirement of multiprotein complexes, including the redox partner (ferredoxins or NADPH reductase for example).[6]