Density functional study on dihydrogen activation at the H cluster in Fe-only hydrogenases

Models simulating the catalytic diiron subcluster FeFe](H) in Fe-only hydrogenases have often been designed for computational exploration of the catalytic mechanism of the formation and cleavage of dihydrogen. In this work, we extended the above models by explicitly considering the electron reservoir 4Fe-4S](H) which is linked to the diiron subcluster to form a whole H cluster (6Fe-6S] = 4Fe-4S](H) + FeFe](H)). Large-scale density functional theory (DFT) computations on the complete H cluster, together with simplified models in which the 4Fe-4S](H) subcluster is not directly involved in the reaction processes, have been performed to probe hydrogen activation on the Fe-only hydrogenases. A new intermediate state containing an Fe(p)...H...CN two-electron three-center bond is identified as a key player in the H2 formation/cleavage processes.