Modeling the signatures of hydrides in metalloenzymes: ENDOR analysis of a Di-iron Fe(μ-NH)(μ-H)Fe core.

ABSTRACT: The application of 35 GHz pulsed EPR and ENDOR spectroscopies has established that the biomimetic model complex L(3)Fe(μ-NH)(μ-H)FeL(3) (L(3) = [PhB(CH(2)PPh(2))(3)](-)) complex, 3, is a novel S = (1)/(2) type-III mixed-valence di-iron II/III species, in which the unpaired electron is shared equally between the two iron centers. (1,2)H and (14,15)N ENDOR measurements of the bridging imide are consistent with an allyl radical molecular orbital model for the two bridging ligands. Both the (μ-H) and the proton of the (μ-NH) of the crystallographically characterized 3 show the proposed signature of a 'bridging' hydride that is essentially equidistant between two 'anchor' metal ions: a rhombic dipolar interaction tensor, T ≈ [T, -T, 0]. The point-dipole model for describing the anisotropic inte

SUBMITTER: Kinney RA 

PROVIDER: S-EPMC3433054 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature