Redox Tuning via Ligand-Induced Geometric Distortions at a YMn(3)O(4) Cubane Model of the Biological Oxygen Evolving Complex

[Image: see text] The function of proteins involved in electron transfer is dependent on cofactors attaining the necessary reduction potentials. We establish a mode of cluster redox tuning through steric pressure on a synthetic model related to Photosystem II. Resembling the cuboidal [CaMn(3)O(4)] subsite of the biological oxygen evolving complex (OEC), [Mn(4)O(4)] and [YMn(3)O(4)] complexes featuring ligands of different basicity and chelating properties were characterized by cyclic voltammetry. In the absence of ligand-induced distortions, increasing the basicity of the ligands results in a decrease of cluster reduction potential. Contraction of Y-oxo/Y–Mn distances by 0.1/0.15 Å enforced by a chelating ligand results in an increase of cluster reduction potential even in the presence of strongly basic donors. Related protein-induced changes in Ca-oxo/Ca–Mn distances may have similar effects in tuning the redox potential of the OEC through entatic states and may explain the cation size dependence on the progression of the S-state cycle.