Cu+/ag+ competition in type i copper proteins (t1cu)

HIGHLIGHTS

SUMMARY

    In respect to the metal center composition, the most abundant amino_acid residues derive from histidine, cysteine and methionine. Both classes lack the fifth amino_acid residue denoted as L2, which renders the resulting geometry of the metal binding center distorted tetrahedral. In the tionalbetween intermolecular hydrogen between the water molecule and BKB-residue construct, the amino_acid residues are arranged in a distorted tetrahedron around the metal cation after the optimization. Without the stronger interaction with an axial amino_acid residue, however, the silver-containing construct becomes linear with Ag-S(Cys) at 2.43 Å and Ag . . .

     

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