Abstract
Metalloproteins represent approximately 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 beta domain and a 11-cysteine alpha 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.
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