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Restricted rotation of an Fe(CO)2(PL3)-subunit in [FeFe]-hydrogenase active site mimics by intramolecular ligation
S. Pullen, , M. Stein, S. Ott
Published in Royal Society of Chemistry
2019
PMID: 30839992
Volume: 48
   
Issue: 18
Pages: 5933 - 5939
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. © 2019 The Royal Society of Chemistry.
About the journal
JournalData powered by TypesetDalton Transactions
PublisherData powered by TypesetRoyal Society of Chemistry
ISSN14779226