Structure—Reactivity Relationships of Metallothionein, a Unique Metal-Binding Protein
Structure—Reactivity Relationships of Metallothionein, a Unique Metal-Binding Protein
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金属硫蛋白（一种独特的金属结合蛋白）的结构-反应性关系
DOI：
10.1080/02603598908035801
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发表时间：
1989
影响因子：
5.4
通讯作者：
C. Shaw
中科院分区：
文献类型：
--
作者：
J. D. Otvos;D. Petering;C. Shaw
抽象的金属氨酸是一种强烈的研究蛋白，它结合了多种必需，有毒和药物活性的金属，包括Zn，CD，AU和PT现在显然，金属氨酸是金属交换和配体替代反应中的一种非常反应性的蛋白本质上的金属和有机物都在其金属的动态特征上找到了基础，这是由113CD NMR技术敏感的。金属硫氨酸的金属结合位点的动力学反应性将其与涉及酶催化的其他典型金属蛋白区分开。这种结构对于其某些已知功能和...显然很重要。
Abstract Metallothionein is an intensively studied protein, which binds a variety of essential, toxic, and pharmacologically active metals, including Zn, Cd, Au, and Pt. Until recently, attention focused primarily on its biological properties and static features of its chemistry. It is now apparent that metallothionein is a remarkably reactive protein in metal exchange and ligand substitution reactions and in its interactions with a number of electrophilic compounds, which are both metallic and organic in nature. This unique behavior finds its basis in the dynamic character of its metal—ligand structure, which is sensitively probed by 113Cd NMR techniques. In an effort to relate the chemistry of metallothionein to its cellular activities, it is shown that the kinetic reactivity of the metal binding sites of metallothionein distinguishes it from other typical metalloproteins involved in enzyme catalysis. The rich inorganic chemistry of this structure is clearly important for some of its known functions and...
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影响因子：
56.9
作者：
KELLEY, SL;BASU, A;LAZO, JS
通讯作者：
LAZO, JS
影响因子：
56.9
作者：
FUREY, WF;ROBBINS, AH;STOUT, CD
通讯作者：
STOUT, CD
艾利希细胞中锌与金属硫蛋白结合的动力学不稳定性。
DOI：
--
发表时间：
1988
期刊：
The Biochemical journal
影响因子：
--
作者：
Krezoski,SK;Villalobos,J;Shaw3rd,CF;Petering,DH
通讯作者：
Petering,DH
艾利希细胞中的锌代谢：金属硫蛋白样锌结合蛋白的特性。
影响因子：
11.2
作者：
Kraker,AJ;Krakower,G;Shaw3rd,CF;Petering,DH;Garvey,JS
通讯作者：
Garvey,JS
影响因子：
10.4
作者：
Petering DH;Fowler BA
通讯作者：
Fowler BA