<p>Nitrogen-fixing organisms perform dinitrogen reduction to ammonia at an iron-M (M = Mo, Fe, or V) cofactor (FeMco) of nitrogenase. FeMoco displays eight metal centers bridged by sulfides and a carbide having the MoFe₇S₈C cluster composition. The role of the carbide ligand, a unique motif in protein active sites, remains poorly understood. Toward addressing its function, we isolated synthetic models of subsite MFe₃S₃C displaying sulfides and a carbyne ligand. We developed synthetic protocols for structurally related clusters, [Tp*MFe₃S₃X]^n-, where M = Mo or W, the bridging ligand X = CR, N, NR, S, and Tp* = tris(3,5-dimethyl-1-pyrazolyl)hydroborate, to study the effects of the identity of the heterometal and the bridging X group on structure and electrochemistry. While the nature of M results in minor changes, the μ₃-bridging ligand X has a large impact on reduction potentials, with differences higher than 1 V, even for the same formal charge, the most reducing clusters being supported by the carbyne ligand. </p>