Characterization of a Diferrous Terminal Hydride Mechanistically Relevant to the Fe-Only Hydrogenases

• Published in: Journal of the American Chemical Society Vol. 127; no. 46; pp. 16012 - 16013
• Main Authors: van der Vlugt, Jarl Ivar, Rauchfuss, Thomas B, Whaley, C. Matthew, Wilson, Scott R
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 23.11.2005
• Subjects: Chemistry; Exact sciences and technology; Ferrous Compounds - chemistry; Ferrous Compounds - metabolism; Hydrogen - chemistry; Hydrogen - metabolism; Hydrogenase - chemistry; Hydrogenase - metabolism; Inorganic chemistry and origins of life; Iron - metabolism; Iron-Sulfur Proteins - chemistry; Iron-Sulfur Proteins - metabolism; Kinetics and mechanism of reactions; Molecular Conformation; Oxidation-Reduction; Spectroscopy, Fourier Transform Infrared; Catalytic reaction; Tertiary phosphine; Organic ligand; Transition metal Carbonyl Complexes; Experimental study; Hydrido complex; Chemical reduction; Infrared spectrometry; Iron Carbonyl Complexes; Complexes Mixed; Dinuclear complex; Reaction mechanism; Hydrogen molecules; Enzymatic type catalysis; Catalyst activity
• ISSN: 0002-7863; 1520-5126
• DOI: 10.1021/ja055475a

Reduction of diferrous dithiolato complexes with hydride donor reagents affords the first example of the previously elusive terminal diferrous hydride, [Fe2(edt)(μ-CO)(H)(CO)(PMe3)4]PF6 (edt = S2C2H4). Crystallographic characterization shows that this model contains an asymmetrical semi-bridging CO trans to a terminal hydrido, as indicated in the Hred state in the D. desulfuricans enzyme. The model reacts with protons to yield H2 and rearranges via an intramolecular process to the isomeric μ-hydrido isomer, which is unreactive toward protons.