A series of diiron complexes based on the [Fe₂Cp₂(CO)_x] skeleton (Cp = η⁵-C₅H₅, x = 2, 3; η⁴-C₅H₅Ph in place of one Cp in one case) and containing different bridging hydrocarbyl ligands (aminocarbyne, thiocarbyne, allenyl) were preliminarily investigated for their anticancer potential. The water solubility, stability in water and in the presence of a cell culture medium, and octanol/water partition coefficient were evaluated by spectroscopic techniques. The cytotoxicity was assessed in vitro toward the human ovarian carcinoma cell line A2780, the human triple negative breast cancer cell line MDA-MB-231, and the human vascular smooth muscle cell line SMC. Some aminocarbyne complexes exhibited a potent cytotoxicity, with IC₅₀ values in the low micromolar/nanomolar range, and a strong selectivity for the A2780 cells in comparison to the SMC cell line. Several experiments were carried out in order to give insight into the mode of action of selected compounds, including an assessment of catalytic NADH oxidation and ROS production and studies of binding with DNA and with a model protein.

DFT has been used to investigate viable mechanisms of the hydrogen evolution reaction (HER) electrocatalyzed by [Fe₂(CN){μ-CN(Me)₂}(μ-CO)(CO)(Cp)₂] (1) in AcOH. Molecular details underlying the proposed ECEC electrochemical sequence have been studied, and the key functionalities of CN^– and amino-carbyne ligands have been elucidated. After the first reduction, CN^– works as a relay for the first proton from AcOH to the carbyne, with this ligand serving as the main electron acceptor for both reduction steps. After the second reduction, a second protonation occurs at CN^– that forms a Fe(CNH) moiety: i.e., the acidic source for the H₂ generation. The hydride (formally 2e/H⁺), necessary to the heterocoupling with H⁺ is thus provided by the μ-CN(Me)₂ ligand and not by Fe centers, as occurs in typical L₆Fe₂S₂ derivatives modeling the hydrogenase active site. It is remarkable, in this regard, that CN^– plays a role more subtle than that previously expected (increasing electron density at Fe atoms). In addition, the role of AcOH in shuttling protons from CN^– to CN(Me)₂ is highlighted. The incompetence for the HER of the related species [Fe₂{μ-CN(Me)₂}(μ-CO)(CO)₂(Cp)₂]⁺ (2⁺) has been investigated and attributed to the loss of proton responsiveness caused by CN^– replacement with CO. In the context of hydrogenase mimicry, an implication of this study is that the dithiolate strap, normally present in all synthetic models, can be removed from the Fe₂ core without loss of HER, but the redox and acid–base processes underlying turnover switch from a metal-based to a ligand-based chemistry. The versatile nature of the carbyne, once incorporated in the Fe₂ scaffold, could be exploited to develop more active and robust catalysts for the HER.