title: ENDOR characterization of a synthetic diiron hydrazido complex as a model for nitrogenase intermediates.
abstract: Molybdenum-dependent nitrogenase binds and reduces N2 at the [Fe7, Mo, S9, X, homocitrate] iron-molybdenum cofactor (FeMo-co). Kinetic and spectroscopic studies of nitrogenase variants indicate that a single Fe-S face is the most likely binding site. Recently, substantial progress has been made in determining the structures of nitrogenase intermediates formed during alkyne and N2 reduction through use of ENDOR spectroscopy. However, constraints derived from ENDOR studies of biomimetic complexes with known structure would powerfully contribute in turning experimentally derived ENDOR parameters into structures for species bound to FeMo-co during N2 reduction. The first report of a paramagnetic Fe-S compound that binds reduced forms of N2 involved Fe complexes stabilized by a bulky beta-diketiminate ligand (Vela, J.; Stoian, S.; Flaschenriem, C. J.; Münck, E.; Holland, P. L. J. Am. Chem. Soc. 2004, 126, 4522-4523). Treatment of a sulfidodiiron(II) complex with phenylhydrazine gave an isolable mixed-valence FeII-Fe(III) complex with a bridging phenylhydrazido (PhNNH2) ligand, and this species now has been characterized by ENDOR spectroscopy. Using both 15N, 2H labeled and unlabeled forms of the hydrazido ligand, the hyperfine and quadrupole parameters of the -N-NH2 moiety have been derived by a procedure that incorporates the (near-) mirror symmetry of the complex and involves a strategy which combines experiment with semiempirical and DFT computations. The results support the use of DFT computations in identifying nitrogenous species bound to FeMo-co of nitrogenase turnover intermediates and indicate that 14N quadrupole parameters from nitrogenase intermediates will provide a strong indication of the nature of the bound nitrogenous species. Comparison of the large 14N hyperfine couplings measured here with that of a hydrazine-derived species bound to FeMo-co of a trapped nitrogenase intermediate suggests that the ion(s) are not high spin and/or that the spin coupling coefficients of the coordinating cofactor iron ion(s) in the intermediate are exceptionally small.
authors: Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, USA.
authors: Nicholas S
authors: NS
authors: Lees
authors: Rebecca L
authors: RL
authors: McNaughton
authors: Wilda Vargas
authors: WV
authors: Gregory
authors: Patrick L
authors: PL
authors: Holland
authors: Brian M
authors: BM
authors: Hoffman
mesh_terms: D004578:Electron Spin Resonance Spectroscopy; D058085:Iron Compounds / Q000737:chemistry*; D008983:Molybdoferredoxin / Q000737:chemistry*; D009591:Nitrogenase / Q000737:chemistry*
chemical_list: D058085:Iron Compounds; D008983:Molybdoferredoxin; D009591:Nitrogenase