The impressive synthetic chemistry that has developed following the elucidation of the organodiiron units within the [FeFe]-H2ase enzyme active site has largely depended on the availability of an easily accessed precursor, (�2-S2)[Fe(CO)3]2.  In reduced bis sulfide form, (�2-S)2[Fe(CO)3]22- , alkylation and condensation at sulfur gives a well known range of products, advancing in the last decade to the more faithful analogues of the [FeFe]-H2ase eas, (�2-SCH2NRCH2)[Fe(CO)2L]2 .  Factors that control the notable flexibility of the latter biomimetics are lacking in the (�2-S2)[Fe(CO)3]2 complexes, despite almost identical electronic characteristics as defined by CO-stretching frequencies.  This report will explore S-reactivity in S-metallated derivatives including CO/L exchange, and metal displacements in LnM(�3-S2) )[Fe(CO)3]2 complexes. Crowie, M.; DeKock, R. L.; Wagenmaker, T. R.; Seyferth, D.; Henderson, R. S.; Gallagher, M. K. Organometallics 1988 , 8, 119-132.Darensbourg, M. Y.; Smee, J. J.; Lyon, E. Coordination Chem. Rev. 2000 , 206-207, 533-561.

Critical precursors to biomimetics of the diiron hydrogenase enzyme active site:  Carbon monoxide mobilized 2Fe2S carbonyl clusters

244th National Meeting (2012)

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