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Title: Mn,Cd-metallothionein-2: A room temperature magnetic protein

Abstract

Naturally occurring metallothionein (MT) is a metal binding protein, which binds to seven Zn{sup 2+} through 20 conserved cysteines and forms two metal binding clusters with a Zinc-Blende structure. We demonstrate that the MT, when substituting the Zn{sup 2+} ions by Mn{sup 2+} and Cd{sup 2+}, 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 Mn{sup 2+} ions inside the clusters. The protein backbone may restrain the net spin moment of Mn{sup 2+} ions from thermal fluctuation. The modified magnetic-metallothionein is a novel approach to creating molecular magnets with operating temperatures up to 330 K.

Authors:
 [1];  [2];  [3];  [4];  [5];  [4];  [5];  [6];  [7]
  1. Department of Biological Science and Technology, National Chiao Tung University, Hsinchu, 300, Taiwan (China) and National Nano Device Laboratories, Hsinchu, 300, Taiwan (China) and Institute of Physics, Academia Sinica, Taipei 11529, Taiwan (China). E-mail: ccchang01@faculty.nctu.edu.tw
  2. Institute of Physics, Academia Sinica, Taipei 11529, Taiwan (China)
  3. Institute of Molecular Science, National Chiao Tung University, Hsinchu, 300, Taiwan (China)
  4. Department of Biological Science and Technology, National Chiao Tung University, Hsinchu, 300, Taiwan (China)
  5. (China)
  6. Institute of Physics, National Chiao Tung University, Hsinchu, 300, Taiwan (China)
  7. Institute of Chemistry, Academia Sinica, Taipei 11529, Taiwan (China). E-mail: lskan@chem.sinica.edu.tw
Publication Date:
OSTI Identifier:
20798812
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 340; Journal Issue: 4; Other Information: DOI: 10.1016/j.bbrc.2005.12.117; PII: S0006-291X(05)02885-8; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CYSTEINE; HYSTERESIS; MAGNETIC MOMENTS; MAGNETIZATION; MANGANESE IONS; METALLOTHIONEIN; SQUID DEVICES; ZINC IONS; ZINC SULFIDES

Citation Formats

Chang, C.-C., Lee, S.-F., Sun, K.-W., Ho, C.-C., Institute of Physics, National Chiao Tung University, Hsinchu, 300, Taiwan, Chen, Y.-T., Institute of Physics, National Chiao Tung University, Hsinchu, 300, Taiwan, Chang, C.-H., and Kan, L.-S. Mn,Cd-metallothionein-2: A room temperature magnetic protein. United States: N. p., 2006. Web. doi:10.1016/j.bbrc.2005.12.117.
Chang, C.-C., Lee, S.-F., Sun, K.-W., Ho, C.-C., Institute of Physics, National Chiao Tung University, Hsinchu, 300, Taiwan, Chen, Y.-T., Institute of Physics, National Chiao Tung University, Hsinchu, 300, Taiwan, Chang, C.-H., & Kan, L.-S. Mn,Cd-metallothionein-2: A room temperature magnetic protein. United States. doi:10.1016/j.bbrc.2005.12.117.
Chang, C.-C., Lee, S.-F., Sun, K.-W., Ho, C.-C., Institute of Physics, National Chiao Tung University, Hsinchu, 300, Taiwan, Chen, Y.-T., Institute of Physics, National Chiao Tung University, Hsinchu, 300, Taiwan, Chang, C.-H., and Kan, L.-S. Fri . "Mn,Cd-metallothionein-2: A room temperature magnetic protein". United States. doi:10.1016/j.bbrc.2005.12.117.
@article{osti_20798812,
title = {Mn,Cd-metallothionein-2: A room temperature magnetic protein},
author = {Chang, C.-C. and Lee, S.-F. and Sun, K.-W. and Ho, C.-C. and Institute of Physics, National Chiao Tung University, Hsinchu, 300, Taiwan and Chen, Y.-T. and Institute of Physics, National Chiao Tung University, Hsinchu, 300, Taiwan and Chang, C.-H. and Kan, L.-S.},
abstractNote = {Naturally occurring metallothionein (MT) is a metal binding protein, which binds to seven Zn{sup 2+} through 20 conserved cysteines and forms two metal binding clusters with a Zinc-Blende structure. We demonstrate that the MT, when substituting the Zn{sup 2+} ions by Mn{sup 2+} and Cd{sup 2+}, 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 Mn{sup 2+} ions inside the clusters. The protein backbone may restrain the net spin moment of Mn{sup 2+} ions from thermal fluctuation. The modified magnetic-metallothionein is a novel approach to creating molecular magnets with operating temperatures up to 330 K.},
doi = {10.1016/j.bbrc.2005.12.117},
journal = {Biochemical and Biophysical Research Communications},
number = 4,
volume = 340,
place = {United States},
year = {Fri Feb 24 00:00:00 EST 2006},
month = {Fri Feb 24 00:00:00 EST 2006}
}