Design of artificial metalloenzymes using non-covalent insertion of a metal complex into a protein scaffold

被引:58
作者
Ueno, Takafumi [1 ]
Koshiyama, Tomomi
Abe, Satoshi
Yokoi, Norihiko
Ohashi, Masataka
Nakajima, Hiroshi
Watanabe, Yoshihito
机构
[1] Nagoya Univ, Res Ctr Mat Sci, Nagoya, Aichi 4648602, Japan
[2] Nagoya Univ, Grad Sch Sci, Dept Chem, Nagoya, Aichi 4648602, Japan
[3] Grad Univ Adv Studies, Dept Struct Mol Sci, Okazaki, Aichi 4448585, Japan
关键词
myoglobin; Schiff base; oxygenation; sulfoxidation; metalloenzyme; heme;
D O I
10.1016/j.jorganchem.2006.08.043
中图分类号
O61 [无机化学];
学科分类号
070301 ; 081704 ;
摘要
Construction of artificial metalloenzymes is one of the most attractive targets in the field of inorganic and catalytic chemistry, since they show remarkable chemoselectivity and reactivity in aqueous media. For the purpose, covalent modification of protein and cofactors have usually been utilized to attach a metal complex(es) to a protein scaffold. This article focuses on non-covalent insertion of metal complexes into protein environments. The discussion includes the screening of stable metal complex/protein composites, crystal structures, molecular design for regulating enantio selectivity of the target catalytic reactions. Our recent results show that the non-covalent conjugation will provide us a new way in semi-synthesis of artificial metalloenzymes. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:142 / 147
页数:6
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