A twisted mimic: Upon oxidation of [(μ-SCH2C(CH3)2CH2S-){FeI(CO)2PMe3}2], rearrangement yields the mixed-valent FeIFeII cation in a square-pyramid/inverted square-pyramid geometry with a semibridging CO ligand, closely mimicking the [FeFe] hydrogenase enzyme active site. According to de novo design principles, the steric effect of bridgehead bulk in the S–S bridging ligand stabilizes this structure in the absence of the protein matrix.
Affiliations
Texas A M University (USA)Department of Chemistry
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Singleton, M., Bhuvanesh, N., Reibenspies, J. H., & Darensbourg, M. Y. (2008). Synthetic support of De Novo design : sterically bulky [FeFe]-hydrogenase models. Angewandte Chemie (International Edition), 47, 9492-9495. https://doi.org/10.1002/anie.200803939 (Original work published 2008)