Determination of the solution three dimensional structure of chemically-synthesized native 113Cd3S9 domain of Lobster Metallothionein by NMR Spectroscopy
Amalia Muņoz*, F. Holger Forsterling, C. Frank Shaw III+ and David H. Petering
Discussion
Stable Cd3betaC cluster was generated when the synthetically prepared native lobster domain was reconstituted with cadmium. Spectroscopic characterization of the cadmium derivative with (1) an absorption band at 250 nm due to MLCT, (2) a CD-signal at ~260 nm due to interactions between asymmetrically coupled pairs of Cd-S unit within the binding site and (3)113Cd-1D NMR chemical shifts between 610 and 670 ppm reflect the formation, at pH~4, of Cd-thiolate clusters analogous to those found in lobster MT. 3D-structure with similar overall folding and conformation to that of the holoprotein. Lobster and mammalian MTs both react in a biphasic fashion with DTNB and EDTA. The rate constants calculated for the native sequence are comparable to those observed for the holoprotein.
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Amalia Muņoz - April, 2000
