Reactivation pathway of the hydrogenase H‐cluster: Density functional theory study |
| |
| Authors: | Stefan Motiu Daniela Dogaru Valentin Gogonea |
| |
| Institution: | 1. Department of Chemistry, Cleveland State University, 2121 Euclid Avenue, Cleveland, Ohio 44115;2. Department of Immunology, Lerner Research Institute, Cleveland Clinic Foundation, 9500 Euclid Avenue, Cleveland, Ohio 44195Department of Chemistry, Cleveland State University, 2121 Euclid Avenue, Cleveland, Ohio 44115 |
| |
| Abstract: | 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. © 2006 Wiley Periodicals, Inc. Int J Quantum Chem, 2007 |
| |
| Keywords: | hydrogenase H‐cluster density functional theory reaction enthalpy bridging carbonyl |
|
|
