Theoretical studies on the redox potentials of Fe dinuclear complexes as models for hydrogenase.

Density Functional calculations have been performed at the uB3LYP and uBP86 levels to calculate the one-electron redox potentials for a series of small models based on the diiron hydrogenase enzymes in the presence of acetonitrile (MeCN). The solvation effects in MeCN are incorporated via a self-consistent reaction field (SCRF) using the polarized continuum model (PCM). The calculated redox potentials reproduce the trends in experimental data with an average error of only 0.12 V using the BP86 functional, whereas comparing results with the B3LYP functional require a systematic shift of -0.82 and -0.53 V for oxidation and reduction, respectively. The bonding orbitals and d-electron populations were examined using Mulliken population analysis, and the results were used to rationalize the calculated and observed redox potentials. These studies demonstrate that the redox potential correlates with the empirical spectrochemical series for the ligands, as well as with the amount of electron density donated by the ligand onto the Fe centers.