Binding of N-2 by nitrogenase requires a reductive activation of the FeMo-cofactor, but the precise structure and atomic composition of FeMoco in its activated form is not well understood. However, recent crystallographic studies suggest that N-2 reduction may occur at a carbon-bridged diiron subunit of FeMoco. Toward modeling the activation of a Fe-(mu-C)-Fe site toward N-2 binding, we synthesized a new dinucleating, hexaphosphine ligand derived from a 2,6-disubstituted toluene platform. Activation of the central methyl group of the ligand affords the diiron ii -carbyne complex (P6ArC) Fe-2(mu-H) featuring a biologically relevant Fe(p-carbyne)(mu-H)Fe motif. SQUID magnetometry, MOssbauer spectroscopy, and DFT calculations reveal that (P6ArC)Fe-2(mu-H) has a well-isolated S = 1 ground state, distinguishing it from all other diiron ii -carbyne complexes which are diamagnetic. Upon the addition of sources of H+/e(-) (H-2, TEMPO-H or HCI), (P6ArC)Fe-2(mu-H) is activated toward N-2 binding, with concomitant protonation of the carbyne ligand. Although reaction with H-2 ultimately leads to complete protonation of the carbyne moiety, mechanistic investigations indicate that formation of a single C-H bond, with concomitant cleavage of one Fe-C bond, generates an iron-carbene intermediate capable of coordinating N-2.