Both biological and industrial nitrogen reduction catalysts activate N-2 at multinuclear binding sites with constrained Fe-Fe distances. This contrasts with molecular diiron systems, which routinely form linear N-2 bridges to minimize steric interactions. Model compounds that capture the salient geometric features of N-2 binding by the nitrogenase enzymes and Mittasch catalysts would contribute to understanding their high N-2-reduction activity. It is shown in the present study that use of a geometrically flexible, dinucleating macrocycle allows for the formation of a bridging N-2 ligand with an unusual Fe-Ct(N2)-Fe angle of 150 degrees (Ct(N2) = centroid of N-2), a geometry that approximates the alpha-N-2 binding mode on Fe(111) surfaces that precedes N-2 bond cleavage. The cavity size of the macrocycle prevents the formation of a linear Fe-N-2-Fe unit and leads to orbital interactions that are distinct from those available to the linear configuration.