Protein-bound [2Fe�2S] sites are fundamental biological cofactors. Their dominant function is electron transfer, where the Fe/S core shuttles between the [Fe2S2]2+ and [Fe2S2]+ states. Synthetic analogues for homoleptic-coordinated [2Fe�2S] cores are well established in bioinorganic chemistry,[1] but most reported analogues of [2Fe�2S] sites have been synthesized exclusively in the all-ferric state. We present the first crystal structure and complete spectroscopic characterization of a mixed valent [2Fe�2S] synthetic analogue[2] as well as the first investigation of an all-ferrous biomimetic [2Fe�2S] species.[3]Furthermore we present synthetic analogues for the Rieske centers which are variants of [2Fe�2S] cofactors with heteroleptic {His2Cys2} ligation. Building upon the first structural Rieske model,[4]we now present functional model systems that also emulate the pH-dependent redox-potentials and the proton coupled electron transfer that has been proposed for some Rieske proteins.[5]References1. P. V. Rao, R. H. Holm, Chem. Rev. 2004  , 104, 527.2. A. Albers, S. Demeshko, S. Dechert, E. Bill, E. Bothe, F. Meyer, Angew. Chem. Int. Ed. 2011  , 50, 9191.3. A. Albers, S. Demeshko, K. Pr�pper, S. Dechert, E. Bill, F. Meyer, J. Am. Chem. Soc. 2013  , 135, 1704.4 J. Ballmann, A. Albers, S. Dechert, E. Bothe, E. Bill, S. Demeshko, F. Meyer, Angew. Chem. Int. Ed. 2008  , 47, 9537.5. A. Albers, T. Bayer, S. Demeshko, S. Dechert, F. Meyer, Chem. Eur. J. 2013 , 19, 10101.

Synthetic analogs for reduced [2Fe-2S] cofactors and for Rieske centers

247th National Meeting (2014)

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