Metal-binding mechanisms in metallothioneins.
Metallothionein are small, cysteine-rich, metal-binding proteins that are found ubiquitously in nature. Most metallothioneins bind multiple metals in two well-defined metal-thiolate clusters. This perspective discusses the use of optical spectroscopy to study the metalation of metallothioneins and the emergence of electrospray ionization mass spectrometry as a means of studying the mechanism of metalation for metallothioneins. A brief history of past kinetic studies of cadmium metallothioneins and recent kinetic study advances for the arsenic metalation of metallothionein will be presented. Lastly, a possible functional role for the two-domain structure of metallothionein will be briefly discussed.
Ngu
Thanh T
TT
Department of Chemistry, The University of Western Ontario, London, CanadaN6A 5B7.
Stillman
Martin J
MJ
D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008668:Metallothionein / Q000737:chemistry / Q000378:metabolism*; D008670:Metals / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D021241:Spectrometry, Mass, Electrospray Ionization
D008670:Metals; D008668:Metallothionein