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  • Title: Structure and vibrational dynamics of model compounds of the [FeFe]-hydrogenase enzyme system via ultrafast two-dimensional infrared spectroscopy.
    Author: Stewart AI, Clark IP, Towrie M, Ibrahim SK, Parker AW, Pickett CJ, Hunt NT.
    Journal: J Phys Chem B; 2008 Aug 14; 112(32):10023-32. PubMed ID: 18646798.
    Abstract:
    Ultrafast two-dimensional infrared (2D) spectroscopy has been applied to study the structure and vibrational dynamics of (mu-S(CH2)3S)Fe2(CO)6, a model compound of the active site of the [FeFe]-hydrogenase enzyme system. Comparison of 2D-IR spectra of (mu-S(CH2)3S)Fe2(CO)6 with density functional theory calculations has determined that the solution-phase structure of this molecule is similar to that observed in the crystalline phase and in good agreement with gas-phase simulations. In addition, vibrational coupling and rapid (<5 ps) solvent-mediated equilibration of energy between vibrationally excited states of the carbonyl ligands of the di-iron-based active site model are observed prior to slower (approximately 100 ps) relaxation to the ground state. These dynamics are shown to be solvent-dependent and form a basis for the future determination of the vibrational interactions between active site and protein.
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