The water-resistant adhesion of mussel adhesive proteins (MAPs) to a wet surface requires a cross-linking step, where the catecholic ligands of MAPs coordinate to various transition-metal ions. Fe(III), among the range of metal ions, induces particularly strong cross-linking. The molecular details underlying this cross-linking mediated by transition-metal ions are largely unknown. Of particular interest is the metalligand binding energy, which is the molecular origin of the mechanical properties of cross-linked MAPs. Using density functional theory, this study examined the structures and binding energies of various trivalent metal ions (TiGa) forming coordination complexes with a polymeric ligand similar to a MAP. These binding energies were 1 order of magnitude larger than the physisorption energy of a catechol molecule on a metallic surface. On the other hand, the coordination strength of Fe(III) with the ligand was not particularly strong compared to the other metal ions studied. Therefore, the strong cross-linking in the presence of Fe(III) is ascribed to its additional ability as an oxidant to induce covalent cross-linking of the catecholic groups of MAPs.