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本文引用的文献

1
Design and engineering of an O(2) transport protein.一种氧运输蛋白的设计与工程
Nature. 2009 Mar 19;458(7236):305-9. doi: 10.1038/nature07841.
2
Harnessing natures ability to control metal ion coordination geometry using de novo designed peptides.利用自然界通过从头设计的肽来控制金属离子配位几何结构的能力。
Dalton Trans. 2009 Apr 7(13):2271-80. doi: 10.1039/b818306f. Epub 2009 Jan 16.
3
The correlation of 113Cd NMR and 111mCd PAC spectroscopies provides a powerful approach for the characterization of the structure of Cd(II)-substituted Zn(II) proteins.113Cd核磁共振与111mCd正电子湮没符合辐射谱学的相关性为表征Cd(II)取代的Zn(II)蛋白质的结构提供了一种强大的方法。
Chemistry. 2009;15(15):3761-72. doi: 10.1002/chem.200802105.
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Engineering a uranyl-specific binding protein from NikR.利用镍调控蛋白构建铀酰特异性结合蛋白。
Angew Chem Int Ed Engl. 2009;48(13):2339-41. doi: 10.1002/anie.200805262.
5
Protein design provides lead(II) ion biosensors for imaging molecular fluxes around red blood cells.蛋白质设计为成像红细胞周围的分子通量提供了铅(II)离子生物传感器。
Biochemistry. 2009 Jan 20;48(2):462-70. doi: 10.1021/bi801777h.
6
Using diastereopeptides to control metal ion coordination in proteins.利用非对映体肽控制蛋白质中的金属离子配位
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7
Biosynthesis of a site-specific DNA cleaving protein.位点特异性DNA切割蛋白的生物合成。
J Am Chem Soc. 2008 Oct 8;130(40):13194-5. doi: 10.1021/ja804653f. Epub 2008 Sep 13.
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One heme, diverse functions: using biosynthetic myoglobin models to gain insights into heme-copper oxidases and nitric oxide reductases.一种血红素,多种功能:利用生物合成肌红蛋白模型深入了解血红素铜氧化酶和一氧化氮还原酶。
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Oxygen reactivity of the biferrous site in the de novo designed four helix bundle peptide DFsc: nature of the "intermediate" and reaction mechanism.从头设计的四螺旋束肽DFsc中双铁位点的氧反应性:“中间体”的性质及反应机制
J Am Chem Soc. 2008 Jul 23;130(29):9188-9. doi: 10.1021/ja801657y. Epub 2008 Jun 24.
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Designed metal-binding sites in biomolecular and bioinorganic interactions.生物分子与生物无机相互作用中设计的金属结合位点。
Curr Opin Struct Biol. 2008 Aug;18(4):484-90. doi: 10.1016/j.sbi.2008.04.009. Epub 2008 Jun 12.

功能性金属蛋白的设计

Design of functional metalloproteins.

作者信息

Lu Yi, Yeung Natasha, Sieracki Nathan, Marshall Nicholas M

机构信息

Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.

出版信息

Nature. 2009 Aug 13;460(7257):855-62. doi: 10.1038/nature08304.

DOI:10.1038/nature08304
PMID:19675646
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2770889/
Abstract

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.

摘要

金属蛋白催化自然界中一些最复杂和重要的过程,如光合作用和水氧化。对我们关于金属蛋白如何工作的知识的最终检验是设计新的金属蛋白。这样做不仅可以揭示天然金属蛋白及其变体研究中可能缺失的隐藏结构特征,还可以产生用于生物技术和制药应用的新金属酶。尽管设计金属蛋白比设计非金属蛋白更具挑战性,但由于计算生物学和结构生物学等领域的最新进展,该领域已经取得了很大进展,特别是在功能设计方面。