Dec 1, 1980

Structure of the metal clusters in rabbit liver metallothionein

Proceedings of the National Academy of Sciences of the United States of America
J D Otvos, I M Armitage

Abstract

Cadmium-113 nuclear magnetic resonance ((113)Cd NMR) has been used to determine the structures of the multiple cadmium binding sites in the two major isoproteins of rabbit liver metallothionein. The isotopically (113)Cd-labeled metallothionein used in these studies was isolated from the livers of rabbits that had been subjected to repeated injections of (113)CdCl(2). The native protein isolated from these livers contains an appreciable amount of Zn in addition to Cd, ranging from 2-3 mol per mol of protein out of a total metal content of 7 mol per mol of protein. The (113)Cd NMR spectrum of Cd, Zn-containing metallothionein is quite complex, reflecting the fact that the native protein is a heterogeneous mixture of species containing different relative amounts of Zn and Cd. Replacement of the native Zn with (113)Cd in vitro gave a protein whose (113)Cd NMR spectrum was much simpler, containing eight distinct multiplets with chemical shifts ranging from 611-670 ppm. The origin of the multiplet structures has been shown to be (113)Cd-(113)Cd scalar coupling arising from two-bond interactions between (113)Cd ions linked to one another by bridging cysteine thiolate ligands. The size and structures of the metal clusters in the protei...Continue Reading

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  • Citations164

References

Mentioned in this Paper

In Vivo NMR Spectroscopy
Magnetic Resonance Imaging
Cadmium Measurement
Metalloproteins
Plasma Protein Binding Capacity
Staphylococcal Protein A
Zinc
Cysteine
Cadmium
Metallothionein IIA

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