International Journal of Quantum Chemistry
This work puts forth a reaction pathway for the reactivation of exogenous ligand inhibited H-cluster, the active site of Fe-only hydrogenases. The H-cluster is a dimetal complex, Fe–Fe, with the metal centers bridged by di(thiomethyl)amine. Exogenous ligands, H2O, and OH−, are bound to the distal iron (Fed). Density functional theory (DFT) calculations on the native and ruthenium-modified H-cluster have been performed using the B3LYP functional with 6-31+G** and 6-311+G** basis sets. We have ascertained that there is a thermodynamically favorable pathway for the reactivation of the OH− inhibited H-cluster, which proceeds by an initial protonation of the Fed–OH− complex. The proposed reaction pathway has all its intermediate reactions ensue exothermically.
Motiu, Stefan; Dogaru, Daniela; and Gogonea, Valentin, "Reactivation Pathway of The Hydrogenase H-cluster: Density Functional Theory Study" (2007). Chemistry Faculty Publications. 326.
This is the accepted version of the following article: Motiu, S.; Dogaru, D.; Gogonea, V. Reactivation pathway of the hydrogenase H-cluster: Density functional theory study. International Journal of Quantum Chemistry 2007, 107, 1248-1252., which has been published in final form at http://onlinelibrary.wiley.com/doi/10.1002/qua.21236/abstract