Restricted rotation of an Fe(CO)2(PL3)-subunit in [FeFe]-hydrogenase active site mimics by intramolecular ligation

Abstract

A new series of homodinuclear iron complexes as models of the [FeFe]-hydrogenase active site was prepared and characterized. The complexes of the general formula [Fe₂(mcbdt)(CO)₅PPh₂R] (mcbdt = benzene-1,2-dithiol-3-carboxylic acid) feature covalent tethers that link the mcbdt ligand with the phosphine ligands which are terminally coordinated to one of the Fe centres. The synthetic feasability of the concept is demonstrated with the preparation of three novel complexes. A detailed theoretical investigation showes that by introducing a rigid covalent link between the phosphine and the bridging dithiolate ligands, the rotation of the Fe(CO)₂P unit is hindered and higher rotation barriers were calculated compared to non-linked reference complexes. The concept of restricting Fe(L)₃ rotation is an approach to kinetically stabilize terminal hydrides which are reactive intermediates in catalytic proton reduction cycles of the enzymes.