Iron complexes of a tris(phosphino)borane ligand as nitrogenase models
- Creators
- Moret, Marc-Etienne
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Peters, Jonas C.
Abstract
Biol. dinitrogen fixation - i.e. The redn. of N_2 to two equiv. of ammonia by addn. of protons and electrons - is thought to proceed through initial coordination of N_2 to one or more iron centers of the nitrogenase MoFe cofactor. To shed light on the mechanism of this transformation, a no. of model compds. have previously been prepd. that mimic the trigonal environment of the iron center in the MoFe cofactor by enforcing either pseudotetrahedral (PT) or trigonal-bipyramidal (TBP) geometry with robust phosphine-based multidentate ligands. In this contribution, we show that both geometries can be accessed in ferraboratranes derived from a tris(phosphino)borane ligands. In particular, we describe terminal iron-N_2 complexes that exhibit a TBP geometry as well as PT compds. with a Fe≡NR triple bond. Efforts towards the functionalization of the ironbound dinitrogen mol. are also discussed.
Additional Information
© 2011 American Chemical Society.Additional details
- Eprint ID
- 47786
- Resolver ID
- CaltechAUTHORS:20140801-104434319
- Created
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2014-08-01Created from EPrint's datestamp field
- Updated
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2019-11-26Created from EPrint's last_modified field