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/sup 113/Cd NMR studies on metal-thiolate cluster formation in rabbit Cd(II)-metallothionein: evidence for a pH dependence

Journal Article · · Biochemistry; (United States)
OSTI ID:6463397

The formation of two metal-thiolate clusters in rabbit liver metallothionein 2 (MT) has been examined by /sup 113/Cd NMR spectroscopy at pH 7.2 and 8.6. The chemical shifts of the /sup 113/Cd resonances developing in the course of apoMT titration with /sup 113/Cd(II) ions have been compared with those of fully metal occupied /sup 113/Cd/sub 7/-MT. At pH 7.2 and at low metal occupancy (<4), a cooperative formation of the four-metal cluster (cluster A) occurs. Further addition of /sup 113/Cd(II) ions generates all the resonances of the three-metal cluster (cluster B) in succession, suggesting cooperative metal binding to this cluster also. In contrast, similar studies at pH 8.6, at low metal occupancy (<4), reveal a broad NMR signal centered at 688 ppm. This observation indicates that an entirely different protein structure exists. When exactly 4 equiv of /sup 113/Cd(II) are bound to apoMP, the /sup 113/Cd NMR spectrum changes to the characteristic spectrum of cluster A. Further addition of /sup 113/Cd(II) ions again leads to the cooperative formation of cluster B. These results stress the determining role of the cluster A domain on the overall protein fold. The observed pH dependence of the cluster formation in MT can be rationalized by the different degree of deprotonation of the cysteine residues (pK/sub a/ approx. 8.9), i.e., by the difference in the Gibbs free energy required to bind Cd(II) ions to the thiolate ligands at both pH values.

Research Organization:
Universitaet Zuerich (Switzerland)
OSTI ID:
6463397
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 27:18; ISSN BICHA
Country of Publication:
United States
Language:
English