Dinitrogen coordination to iron centers underpins industrial and biological fixation in the Haber-Bosch process and by the FeM cofactors in the nitrogenase enzymes. The latter employ local high-spin metal centers; however, iron-dinitrogen coordination chemistry remains dominated by low-valent states, contrasting the enzyme systems. Here, we report a highspin mixed-valent cis-, where [L bis ] À is a bis(βdiketiminate) cyclophane. Field-applied Mössbauer spectra, dc and ac magnetic susceptibility measurements, and computational methods support a delocalized S = 7 / 2 Fe 2 N 2 unit with D = À 5.23 cm À 1 and consequent slow magnetic relaxation.Converting atmospheric dinitrogen into bioavailable forms (e.g., NH 3 ) is essential to life on Earth. However, scission of dinitrogen is a kinetically-limited reaction. [1] The Haber-Bosch process for industrial production of NH 3 employs the iron-based Mittasch catalyst and high temperatures and pressures to achieve reductive cleavage of N 2 . [2] Contrastingly, nitrogenase enzymes in biological systems effect N 2 reduction to NH 3 under ambient conditions utilizing Fe 7 M (M = Mo, V or Fe) cofactors with local high-spin Fe centers. [3] Whereas iron reactive sites in the Mittasch catalyst are predominantly in reduced states, [2] the nitrogenase cofactors are proposed to employ a cluster with minimal, if any, low valent iron character for N 2 conversion to NH 3 . [4][5][6][7]