Oxidation Catalysis by Rationally Designed Artificial Metalloenzymes

Oxidation Catalysis by Rationally Designed Artificial Metalloenzymes
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合理设计的人工金属酶的氧化催化

DOI:
10.1002/ijch.201400110
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发表时间:
2015
影响因子:
3.2
通讯作者:
S. Ménage
S. Ménage
中科院分区:
化学3区
文献类型:
--
作者:
Caroline Marchi‐Delapierre;Laurianne Rondot;C. Cavazza;S. Ménage

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通过设计嵌入生物分子中的无机复合物制成的杂交体,酶模拟物的原理已经达到了顶峰。本文综述了人工金属酶的设计及其在氧化反应中的应用,特别是通过超分子相互作用锚定无机络合物或金属离子的蛋白质。这些反应对于结构单元的有机合成具有极大的意义。在第一部分中,人工酶的不同设计的概述之后,审查提出了贡献的合理设计的有效的混合生物催化剂通过超分子主/客体的方法,基于无机复合物的性质和蛋白质的性质,特别注意底物结合。在第二部分中,人工金属酶的最初目的被扭曲为能够观察瞬时中间体,以破译金属氧化机制。由于X射线晶体学,宿主蛋白质晶体已被用作晶体分子尺度的容器,在该容器内进行无机催化反应。这些杂合体应该是酶的替代物用于酶促化学。
The principle of enzyme mimics has been raised to its pinnacle by the design of hybrids made from inorganic complexes embedded into biomolecules. The present review focuses on the design of artificial metalloenzymes for oxida- tion reactions by oxygen transfer reactions, with a special focus on proteins anchoring inorganic complexes or metal ions via supramolecular interactions. Such reactions are of great interest for the organic synthesis of building blocks. In the first part, following an overview of the different design of artificial enzymes, the review presents contributions to the rational design of efficient hybrid biocatalysts via supra- molecular host/guest approaches, based on the nature of the inorganic complex and the nature of the protein, with special attention to the substrate binding. In the second part, the original purpose of artificial metalloenzymes has been twisted to enable the observation of transient inter- mediates, to decipher metal-based oxidation mechanisms. The host protein crystals have been used as crystalline mo- lecular-scale vessels, within which inorganic catalytic reac- tions have been followed, thanks to X-ray crystallography. These hybrids should be an alternative to enzymes for sus- tainable chemistry.
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发表时间: 2011-02-01
期刊: BIOCHEMISTRY
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