Fast electron transfer of blue copper proteins is recognized and attributed to the highly constrained copper sites. Known as the “rack” or “entatic” states, the distorted geometries in copper proteins are adapted to minimize reorganization energies when switching between oxidation states. To understand the structural effects on electron transfer rates comparative to those of copper proteins, a family of highly constrained square planar Cu (I) complexes were synthesized. Although unusual for the d<sup>10</sup> configuration, square planar Cu (I) compounds are synthetically accessible by using pincer-type pyridinediimine (PDI) ligands. These monomeric compounds were confirmed to be in the Cu (I) state by NMR and X-ray crystallography. The later revealed that the PDI Cu (I) compounds were distorted square planar, quantified by τ<sub>4</sub> values derived from the bond angles around the copper center.

Square planar copper (I) complexes with geometric constraints pertinent to copper proteins

253rd National Meeting (2017)

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