Design and engineering of artificial oxygen-activating metalloenzymes

被引：140
作者：
Nastri, Flavia [1 ]
Chino, Marco [1 ]
Maglio, Ornella [1 ,2 ]
Bhagi-Damodaran, Ambika [3 ]
Lu, Yi [3 ]
Lombardi, Angela [1 ]
机构：
[1] Univ Naples Federico II, Dept Chem Sci, Via Cintia, I-80126 Naples, Italy
[2] CNR, IBB, Via Mezzocannone 16, I-80134 Naples, Italy
[3] Univ Illinois, Dept Chem, A322 CLSL,600 South Mathews Ave, Urbana, IL 61801 USA
来源：
CHEMICAL SOCIETY REVIEWS | 2016年 / 45卷 / 18期
基金：
美国国家科学基金会; 美国国家卫生研究院;
关键词：
DE-NOVO DESIGN; CYTOCHROME-C PEROXIDASE; UNNATURAL AMINO-ACIDS; CARBOXY-SUBSTITUTED TETRAARYLPORPHYRIN; HEME OCTAPEPTIDE MICROPEROXIDASE-8; PSEUDOMONAS-AERUGINOSA AZURIN; NONHEME IRON ENZYMES; 2-HIS-1-CARBOXYLATE FACIAL TRIAD; BIOTIN-STREPTAVIDIN TECHNOLOGY; METAL-ORGANIC FRAMEWORKS;
D O I：
10.1039/c5cs00923e
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Many efforts are being made in the design and engineering of metalloenzymes with catalytic properties fulfilling the needs of practical applications. Progress in this field has recently been accelerated by advances in computational, molecular and structural biology. This review article focuses on the recent examples of oxygen-activating metalloenzymes, developed through the strategies of de novo design, miniaturization processes and protein redesign. Considerable progress in these diverse design approaches has produced many metal-containing biocatalysts able to adopt the functions of native enzymes or even novel functions beyond those found in Nature.
引用
收藏
页码：5020 / 5054
页数：35
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