Model compound met the key structural and spectroscopic features of [FeFe]-hydrogenase active site
Biomimetic synthesis of the [FeFe]-hydrogenase active site draws considerable attention of scientists for its amazing catalytic efficiency on reversible transition between proton and hydrogen. Fe2(CO)3[μ-(SCH(CH2CH3)CH2S)](μ-DPPM)(κ1-DPPM) (compound 1) which replicated key structural aspects of the natural [FeFe]-hydrogenase was designed and synthesized. 1 showed that the wavenumbers in IR were close to those of the natural [FeFe]-hydrogenase active site. In addition, 1 achieved the low oxidation potentials at -0.48 V and -0.26 V, respectively. In the assistance of ethyl located in the S-S bridging structure, the asymmetrical substitution with sterically encumbering and electron-rich ligands in 1 may offer a thorough protection for forming and stabilizing the open site in the rotated structure.