Low temperature magnetic circular dichroism (LT MCD) spectroscopy in combinatiori with quantum-chemical calculations are used to define the electronic structure associated with the geometric structure of the Fe-IV=O intermediate in SyrB2 that was previously determined by nuclear resonance vibrational spectroscopy. These studies elucidate key frontier molecular orbitals (FMOs) and their contribution to H atom abstraction reactivity. The VT MCD spectra of the enzymatic S = 2 Fe-IV=O intermediate with Br- ligation contain information-rich features that largely parallel the corresponding spectra of the S = 2 model complex (TMG(3)tren)Fe-IV=O (Srnec, M.; Wong, S. D.; England, j.; Que, L. Jr.; Solomon, E. I. Proc. Natl. Acad. Sci. USA 2012, 109, 14326-14331). However, quantitative differences are observed that correlate with pi-anisotropy and oxo donor strength that perturb FMOs and affect reactivity. Due to pi-anisotropy, the Fe-IV=O active site exhibits enhanced reactivity in the direction of the substrate cavity that proceeds through a pi-channel that is controlled by perpendicular orientation of the substrate C-H bond relative to the halide-Fe-IV=O plane. Also, the increased intrinsic reactivity of the SyrB2 intermediate relative to the ferryl model complex is correlated to a higher oxyl Character of the Fe-IV=O at the transition states resulting from the weaker ligand field of the halogenase.