Structure and vibrational dynamics of model compounds of the [FeFe]−hydrogenase enzyme system via ultrafast two-dimensional infrared spectroscopy

A. I. Stewart, I. P. Clark, M. Towrie, S. K. Ibrahim, A. W. Parker, C. J. Pickett, N. T. Hunt

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37 Citations (Scopus)


Ultrafast two-dimensional infrared (2D) spectroscopy has been applied to study the structure and vibrational dynamics of (µ-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 (µ-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 (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.
Original languageEnglish
Pages (from-to)10023-10032
Number of pages10
JournalThe Journal of Physical Chemistry B
Issue number32
Publication statusPublished - 2008

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