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Bioinorganic Chemistry and Applications
Volume 2010, Article ID 541829, 6 pages
Research Article

The Zn- or Cu-Thionein Character of a Metallothionein Determines Its Metal Load When Synthesized in Physiological (Metal-Unsupplemented) Conditions

1Departament de Química, Facultat de Ciències, Universitat Autònoma de Barcelona, 08193 Cerdanyola del Vallès (Barcelona), Spain
2Departament de Genètica, Facultat de Biologia, Universitat de Barcelona, Institut de Biomedicina de la Universitat de Barcelona (IBUB), 08028 Barcelona, Spain

Received 11 December 2009; Accepted 26 February 2010

Academic Editor: Spyros Perlepes

Copyright © 2010 Mercè Capdevila et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The present work comprises the recombinant synthesis of four metallothioneins (MTs) in metal-unsupplemented cultures and the characterization of the recovered metal complexes by means of analytical and spectrometric techniques. The four MTs are two Drosophila (MtnA and MtnB), one yeast (Crs5), and one mouse (mMT1) metallothionein isoforms. These four MTs exhibit distinct metal binding preferences, from a clear Cu-thionein character to a definite Zn-thionein nature, respectively. Although in all cases, the only metal ion present in the purified complexes is , our results highlight an inherently different behaviour of those two types of MTs, in conditions that would mimic their synthesis in physiological environments. Therefore, intrinsically different roles can be hypothesized for the constitutively-produced MT peptides in the absence of any metal overload, depending on their Zn- or Cu-thionein character.