Mn,Cd-metallothionein-2: A room temperature magnetic protean

被引：6

作者：

Chang, CC ^{[1
]}

Lee, SF

Sun, KW

Ho, CC

Chen, YT

Chang, CH

Kan, LS

机构：

[1] Natl Chiao Tung Univ, Dept Biol Sci & Technol, Hsinchu 300, Taiwan

[2] Natl Nanodevice Labs, Hsinchu 300, Taiwan

[3] Acad Sinica, Inst Phys, Taipei 11529, Taiwan

[4] Natl Chiao Tung Univ, Inst Mol Sci, Hsinchu 300, Taiwan

[5] Natl Chiao Tung Univ, Inst Phys, Hsinchu 300, Taiwan

[6] Acad Sinica, Inst Chem, Taipei 11529, Taiwan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 340卷 / 04期

关键词：

metallothionein; Zinc-Blende structure; magnetization; double exchange; hysteresis cycle; molecular magnet;

D O I：

10.1016/j.bbrc.2005.12.117

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Naturally occurring metallothionein (MT) is a metal binding protein, which binds to seven Zn2+ through 20 conserved cysteines and forms two metal binding clusters with a Zinc-Blende structure. We demonstrate that the MT, when substituting the Zn2+ ions by Mn2+ and Cd2+, exhibits magnetic hysteresis loop observable by SQUID from 10 to 330 K. The magnetic moment may have originated from the bridging effect of the sulfur atoms between the metal ions that leads to the alignment of the electron spins of the Mn2+ ions inside the clusters. The protein backbone may restrain the net spin moment of Mn2+ ions from thermal fluctuation. The modified magnetic-metallothionein is a novel approach to creating molecular magnets with operating temperatures up to 330 K. (c) 2005 Elsevier Inc. All rights reserved.

引用

页码：1134 / 1138

页数：5

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