Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 112, Issue 32, Pages 10023-10032Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp803338d
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Funding
- Engineering and Physical Sciences Research Council [EP/D071011/1] Funding Source: researchfish
- EPSRC [EP/D071011/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council Funding Source: Medline
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Ultrafast two-dimensional infrared (2D) spectroscopy has been applied to study the structure and vibrational dynamics of (mu-S(CH2)(3)S)Fe-2(CO)(6), a model compound of the active site of the [FeFe]-hydrogenase enzyme system. Comparison of 2D-IR spectra of (mu-S(CH2)(3)S)Fe-2(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 (similar to 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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