Redox Tuning via Ligand-Induced Geometric Distortions at a YMnO Cubane Model of the Biological Oxygen Evolving Complex.

08:00 EDT 16th May 2019 | BioPortfolio

Summary of "Redox Tuning via Ligand-Induced Geometric Distortions at a YMnO Cubane Model of the Biological Oxygen Evolving Complex."

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 [CaMnO] subsite of the biological oxygen evolving complex (OEC), [MnO] and [YMnO] 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.


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Name: Inorganic chemistry
ISSN: 1520-510X


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