A new breakthrough for zinc (II) enzyme models was achieved with the advent of macrocyclic polyamine zinc (II) complexes. These complexes serve as the best structural as well as functional model for the active centers of zinc (II) enzymes (e.g., carbonic anhydrase, alkaline phosphatase, and alcohol dehydrogenase) and have clearly answered mysteries surrounding the intrinsic properties of zinc (II) in the zinc (II) enzymes. The knowledge newly gained about the properties of zinc (II) has been developed into new supramolecular chemistry, where the zinc (II) enzyme model complexes can recognize thymine and its related derivatives among all the nucleobases in aqueous solution. Here new biochemical functions of the zinc complexes (i.e., inhibition of hybridization of polyribonucleic acids, inhibition of in vitro protein synthesis, inversion of DNA helicity, etc.) are also presented.