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Diversity of Cluster Structures in Mammalian Metallothionein: Interplay Between Metal Ions and Polypeptide Chain

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Cytotoxic, Mutagenic and Carcinogenic Potential of Heavy Metals Related to Human Environment

Part of the book series: NATO ASI Series ((ASEN2,volume 26))

Abstract

After introducing the 3D structure of mammalian metallothioneins (MTs), a class of low molecular weight metal-binding proteins, spectroscopic evidence for the metal selectivity of clusters and their structural changes upon binding of different divalent metal ions is presented. An interplay between both the chemistry of metal ions and the steric requirements of the polypeptide chain as the cause of the diversity of the metal-thiolate cluster structures in MT is discussed. Moreover, a metal-assisted ligand (apoMT) preorganization as a general concept for the formation of MT structure has been proposed.

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Authors and Affiliations

  1. Biochemisches Institut der Universität Zürich, Winterthurerstrasse 190, CH-8057, Zürich, Switzerland

    M. Vašák & R. Bogumil

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  1. M. Vašák
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  2. R. Bogumil
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  1. Laboratory of Inorganic and General Chemistry, Department of Chemistry, University of Ioannina, Ioannina, Greece

    Nick D. Hadjiliadis

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Vašák, M., Bogumil, R. (1997). Diversity of Cluster Structures in Mammalian Metallothionein: Interplay Between Metal Ions and Polypeptide Chain. In: Hadjiliadis, N.D. (eds) Cytotoxic, Mutagenic and Carcinogenic Potential of Heavy Metals Related to Human Environment. NATO ASI Series, vol 26. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5780-3_10

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  • DOI: https://doi.org/10.1007/978-94-011-5780-3_10

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-6440-8

  • Online ISBN: 978-94-011-5780-3

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