Favorable Protonation of the (μ‐edt)[Fe 2 (PMe 3 ) 4 (CO) 2 (H‐terminal)] + Hydrogenase Model Complex Over Its Bridging μ‐H Counterpart: A Spectroscopic and DFT Study

The mechanism of hydrogen production in [FeFe] hydrogenase remains elusive. However, a species featuring a terminal hydride bound to the distal Fe is thought to be the key intermediate leading to hydrogen production. In this study, density functional theory (DFT) calculations on the terminal ( H ‐term) and bridging (μ‐H) hydride isomers of (μ‐edt)[Fe 2 (PMe 3 ) 4 (CO) 2 H] + are presented in order to understand the factors affecting their propensity for protonation. Relative to H ‐term, μ‐H is 12.7 kcal/mol more stable, which contributes to its decreased reactivity towards an acid. Potential energy surface (PES) calculations for the reaction of the H ‐term isomer with 4‐nitropyridinium, a proton source, further reveal a lower activation energy barrier (14.5 kcal/mol) for H ‐term than for μ‐H (29 kcal/mol). Besides these energetic considerations, the H ‐term isomer displays a key molecular orbital (MO <139>) that has a relatively strong hydride (1s) contribution (23 %), which is not present in the μ‐H isomer. This indicates a potential orbital control of the reaction of the hydride complexes with acid. The lower activation energy barrier and this key MO together control the overall catalytic activity of (μ‐edt)[Fe 2 (PMe 3 ) 4 (CO) 2 (H‐term)] + . Lastly, Raman and IR spectroscopy were performed in order to probe the ν (Fe‐H) stretching mode of the two isomers and their deuterated counterparts. A ν (Fe‐H) stretching mode was observed for the μ‐H complex at 1220 cm –1 . However, the corresponding mode is not observed for the less stable H ‐term isomer.