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, Neil T. Hunt

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)10023-10032
Number of pages10
JournalJournal of Physical Chemistry B
Volume112
Issue number32
DOIs
Publication statusPublished - 14 Aug 2008

Keywords

  • effective core potentials
  • 2d ir spectroscopy
  • echo correlation spectroscopy
  • effect ohd-oke
  • molecular calculations
  • 2d-ir spectroscopy
  • only hydrogenase
  • time
  • transition
  • evolution

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