[superscript 19]F NMR Study of Ligand Dynamics in Carboxylate-Bridged Diiron(II) Complexes Supported by a Macrocyclic Ligand
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Author(s)
Minier, Mikael Antoine
Lippard, Stephen J.
Alternative Title
19F NMR study of ligand dynamics in carboxylate-bridged diiron(II) complexes supported by a macrocyclic ligand
Date Issued
September 2015
Journal
Dalton Transactions
Publisher
Royal Society of Chemistry
Citation
Minier, Mikael A., and Stephen J. Lippard. “[superscript 19]F NMR Study of Ligand Dynamics in Carboxylate-Bridged Diiron(II) Complexes Supported by a Macrocyclic Ligand.” Dalton Trans. 44.41 (2015): 18111–18121.
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Author's final manuscript
Abstract
A series of asymmetrically carboxylate-bridged diiron(II) complexes featuring fluorine atoms as NMR spectroscopic probes, [Fe[subscript 2](PIM)(Ar[superscript 4F-Ph]CO[subscript 2])[subscript 2]] (10), [Fe[subscript 2](F[subscript 2]PIM)(Ar[superscript Tol]CO[subscript 2])[subscript 2]] (11), and [Fe[subscript 2](F[subscript 2]PIM)(Ar[superscript 4F-Ph]CO[subscript 2])[superscript 2]] (12), were prepared and characterized by X-ray crystallography, Mössbauer spectroscopy, and VT [superscript19]F NMR spectroscopy. These complexes are part of a rare family of syn-N diiron(II) complexes, [Fe[subscript 2](X[subscript 2]PIM)(RCO[subscript 2])[superscript 2]], that are structurally very similar to the active site of the hydroxylase enzyme component of reduced methane monooxygenase (MMOH[subscript red]). Solution characterization of these complexes demonstrates that they undergo intramolecular carboxylate rearrangements, or carboxylate shifts, a dynamic feature relevant to the reactivity of the diiron centers in bacterial multicomponent monooxygenases
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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DOI of Published Version
https://doi.org/10.1039/c5dt02138c
