✦ LIBER ✦

Metalation of metallothioneins

✍ Scribed by Thanh T. Ngu; Martin J. Stillman

Publisher: John Wiley and Sons
Year: 2009
Tongue: English
Weight: 603 KB
Volume: 61
Category: Article
ISSN: 1521-6543
DOI: 10.1002/iub.182

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✦ Synopsis

Abstract

Metalloproteins represent ∼30% of all proteins known, yet our understanding of the structures of these metalloproteins, the metal content, and the mechanism for metalation are still very limited. One of the most studied metalloproteins is the ubiquitous metallothionein (MT), which in mammals contains two metal‐binding domains: a 9‐cysteine β domain and a 11‐cysteine α domain. Metals are coordinated in MT via the cysteinyl thiols present in the primary amino acid sequence and the geometry is controlled by the metal ion. This short review discusses the use of optical spectroscopy to study the metalation of MT with particular emphasis on the benefits and pitfalls involved. Further, the new properties of MT that have been revealed using electrospray ionization mass spectrometry in recent metalation studies will also be discussed. © 2009 IUBMB IUBMB Life, 61(4):438–446, 2009

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