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Special Issue "Metallothioneins in Bioinorganic Chemistry: Recent Developments"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Bioinorganic Chemistry".

Deadline for manuscript submissions: 16 April 2017

Special Issue Editor

Guest Editor
PD. Dr. Eva Freisinger

Department of Chemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland
Website | E-Mail
Phone: +41 44 63 546 21
Interests: structures and properties of plant metallothioneins; gene cloning, protein over-expression, and purification; spectroscopic and biochemical characterization of MTs; determination of metal ion binding affinities and redox states; structure determination of MTs by X-ray and NMR

Special Issue Information

Dear Colleagues,

“Metallothioneins”—this is the name of a superfamily combining proteins with two rather basic characteristics, a high percentage of thiolate groups in form of cysteine residues and the ability to coordinate certain metal ions via these thiolate ligands. There is, however, no requirement for a specific function or structure. While the name was initially invented 60 years ago for a class of proteins found in mammalians, all having very similar sequences and a common three-dimensional structure involving metal-thiolate clusters, nowadays, proteins from nearly all kingdoms of life, among them vertebrates, molluscs, nematodes, prokaryotes, fungi, and plants are included. Often the classification as metallothionein is solely based on the respective gene sequence without further knowledge about the metal ion binding ability of the encoded protein. The elucidation of the metal ion binding modes including cluster formation, the spectroscopic properties and last not least the three-dimensional structures of the members of this very variable superfamily belongs to the classical research fields of Bioinorganic Chemistry. Beyond this basic characterisation, unravelling the diversity of functions including, but not being restricted to, metal ion homeostasis and detoxification as well as redox activities, investigating the role of MTs in certain diseases, and inventing biotechnological applications are hot topics in MT research.

It is the aim of this Special Issue to highlight the recent developments in the field in form of Topical Reviews, Articles, and Short Communications. I invite you all to make this Special Issue a valuable source of new and exciting information about this very unique protein superfamily.

PD. Dr. Eva Freisinger
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.


•    metallothioneins (MTs)
•    metal clusters
•    zinc
•    cadmium
•    copper
•    metal ion homeostasis
•    heavy metal detoxification
•    reactive oxygen species  (ROS) scavenging
•    spectroscopy

Published Papers (1 paper)

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Open AccessArticle The Application of Curve Fitting on the Voltammograms of Various Isoforms of Metallothioneins–Metal Complexes
Int. J. Mol. Sci. 2017, 18(3), 610; doi:10.3390/ijms18030610
Received: 11 February 2017 / Revised: 3 March 2017 / Accepted: 7 March 2017 / Published: 11 March 2017
PDF Full-text (1380 KB) | HTML Full-text | XML Full-text | Supplementary Files
The translation of metallothioneins (MTs) is one of the defense strategies by which organisms protect themselves from metal-induced toxicity. MTs belong to a family of proteins comprising MT-1, MT-2, MT-3, and MT-4 classes, with multiple isoforms within each class. The main aim of
[...] Read more.
The translation of metallothioneins (MTs) is one of the defense strategies by which organisms protect themselves from metal-induced toxicity. MTs belong to a family of proteins comprising MT-1, MT-2, MT-3, and MT-4 classes, with multiple isoforms within each class. The main aim of this study was to determine the behavior of MT in dependence on various externally modelled environments, using electrochemistry. In our study, the mass distribution of MTs was characterized using MALDI-TOF. After that, adsorptive transfer stripping technique with differential pulse voltammetry was selected for optimization of electrochemical detection of MTs with regard to accumulation time and pH effects. Our results show that utilization of 0.5 M NaCl, pH 6.4, as the supporting electrolyte provides a highly complicated fingerprint, showing a number of non-resolved voltammograms. Hence, we further resolved the voltammograms exhibiting the broad and overlapping signals using curve fitting. The separated signals were assigned to the electrochemical responses of several MT complexes with zinc(II), cadmium(II), and copper(II), respectively. Our results show that electrochemistry could serve as a great tool for metalloproteomic applications to determine the ratio of metal ion bonds within the target protein structure, however, it provides highly complicated signals, which require further resolution using a proper statistical method, such as curve fitting. Full article
(This article belongs to the Special Issue Metallothioneins in Bioinorganic Chemistry: Recent Developments)

Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Proteomic Zn2+ Trafficking:  Where Does Metallothionein Fit in?
Petering et al.

Mammalian metallothionein-3: new functional and structural insights
Vasak et al.

In depth analysis of the metal binding abilities of Ll-MT (Litorina littorea metallothionein) and two truncated mutants
Capdevila et al.

In depth analysis of the metal binding abilities of BgMT (Biomphalaria glabrata metallothionein) and two crucial, natural  (CY and KN) mutants
Capdevila et al.

cDNA sequence, protein expression and metal binding properties of metallothionein from wild populations of the catfish Clarias gariepinus: Potential as biomarker for metal pollution of Zambia’s Kafue River
Blindauer et al.

The structures of human metallothioneins and their functions in human zinc metabolism
Maret et al.

Regulation of MT3 by a variety of metal ions in human neuronal cell cultures
Austin et al.

Earthworm MT
Höckner et al.

Residue modification analyzed by ESI-MS for the investigation of structural and metallation properties of metallothioneins and other proteins
Stillman et al.

The application of curve fitting on the voltammograms of various isoforms of metallothioneins-metal complexes
Vojtech et al.

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