Light-Emitting Self-Assembled Materials Based on d(8) and d(10) Transition Metal Complexes.

Reactive and potentially toxic cofactors such as copper ions are imported into eukaryotic cells and incorporated into target proteins by unknown mechanisms. Atx1, a prototypical copper chaperone protein from yeast, has now been shown to act as a soluble cytoplasmic copper(I) receptor that can adopt either a two- or three-coordinate metal center in the active site. Atx1 also associated directly with the Atx1-like cytosolic domains of Ccc2, a vesicular protein defined in genetic studies as a member of the copper-trafficking pathway. The unusual structure and dynamics of Atx1 suggest a copper exchange function for this protein and related domains in the Menkes and Wilson disease proteins.

https://science.sciencemag.org/content/sci/278/5339/853.full.pdf

Metal ion chaperone function of the soluble Cu(I) receptor Atx1.

The structural chemistry of metal thiolate complexes

Thiolato-complexes of the transition metals

The Hah1 metallochaperone protein is implicated in copper delivery to the Menkes and Wilson disease proteins. Hah1 and the N-termini of its target proteins belong to a family of metal binding domains characterized by a conserved MT/HCXXC sequence motif. The crystal structure of Hah1 has been determined in the presence of Cu(I), Hg(II), and Cd(II). The 1.8 A resolution structure of CuHah1 reveals a copper ion coordinated by Cys residues from two adjacent Hah1 molecules. The CuHah1 crystal structure is the first of a copper chaperone bound to copper and provides structural support for direct metal ion exchange between conserved MT/HCXXC motifs in two domains. The structures of HgHah1 and CdHah1, determined to 1.75 A resolution, also reveal metal ion coordination by two MT/HCXXC motifs. An extended hydrogen bonding network, unique to the complex of two Hah1 molecules, stabilizes the metal binding sites and suggests specific roles for several conserved residues. Taken together, the structures provide models for intermediates in metal ion transfer and suggest a detailed molecular mechanism for protein recognition and metal ion exchange between MT/HCXXC containing domains.

Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins.

Metal-mercaptide chemistry. The synthesis and structural characterization of the [Cu(SC6H5)3]2- anion. A rational synthesis and the structure of the [Cu4(SC6H5)6]2- cluster

C. N. Murphy

Papers

Metal-mercaptide chemistry. The synthesis and structural characterization of the [Cu(SC6H5)3]2- anion. A rational synthesis and the structure of the [Cu4(SC6H5)6]2- cluster