Metallothioneins in Bioinorganic Chemistry: Recent Developments

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

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