Design of functional metalloproteins

被引：590

作者：

Lu, Yi ^{[1
]}

Yeung, Natasha ^{[1
]}

Sieracki, Nathan ^{[1
]}

Marshall, Nicholas M. ^{[1
]}

机构：

[1] Univ Illinois, Dept Chem, Urbana, IL 61801 USA

来源：

NATURE | 2009年 / 460卷 / 7257期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

DE-NOVO DESIGN; 3-STRANDED COILED COILS; UNNATURAL AMINO-ACIDS; HEME-COPPER OXIDASES; GREEN FLUORESCENT PROTEIN; METAL-ION COORDINATION; BINDING-PROTEIN; ARTIFICIAL METALLOENZYMES; ELECTRON-TRANSFER; 4-HELIX BUNDLE;

D O I：

10.1038/nature08304

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Metalloproteins catalyse some of the most complex and important processes in nature, such as photosynthesis and water oxidation. An ultimate test of our knowledge of how metalloproteins work is to design new metalloproteins. Doing so not only can reveal hidden structural features that may be missing from studies of native metalloproteins and their variants, but also can result in new metalloenzymes for biotechnological and pharmaceutical applications. Although it is much more challenging to design metalloproteins than non-metalloproteins, much progress has been made in this area, particularly in functional design, owing to recent advances in areas such as computational and structural biology.

引用

收藏

页码：855 / 862

页数：8

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