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Mercury(II) binding to metallothionein in Mytilus edulis revealed by high energy-resolution XANES spectroscopy.

Of all divalent metals, mercury (Hg(II)) has the highest affinity for metallothioneins. Hg(II) is considered to be enclosed in the α and β domains as tetrahedral α-type Hg4Cys11-12 and β-type Hg3Cys9 clusters similarly to Cd(II) and Zn(II). However, neither the four-fold coordination of Hg nor the existence of Hg-Hg atomic pairs have ever been demonstrated, and the Hg(II) partitioning among the two protein domains is unknown. Using high energy-resolution XANES spectroscopy, MP2 geometry optimization, and biochemical analysis, we provide evidence for the coexistence of two-coordinate Hg-thiolate complex and four-coordinate Hg-thiolate cluster with a metacinnabar-type (β-HgS) structure in the α domain of separate metallothionein molecules from blue mussel under in vivo exposure. The findings suggest that the CXXC claw setting of thiolate donors, which only exists in the α domain, acts as a nucleation center for the polynuclear complex and that the five CXC motifs from this domain serve as the cluster-forming motifs. Oligomerization is driven by metallophilic Hg-Hg interactions. Our results provide clues as to why Hg has higher affinity for the α than the β domain. More generally, they provide a foundation for understanding how metallothioneins mediate mercury detoxification in the cell under in vivo conditions.

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