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

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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.
LanguageEnglish
Pages10023-10032
Number of pages10
JournalJournal of Physical Chemistry B
Volume112
Issue number32
DOIs
Publication statusPublished - 14 Aug 2008

Fingerprint

Hydrogenase
Carbon Monoxide
enzymes
Infrared spectroscopy
Enzymes
infrared spectroscopy
Phase structure
Excited states
Ground state
Density functional theory
Iron
Gases
Ligands
Crystalline materials
Proteins
Molecules
vapor phases
density functional theory
proteins
iron

Keywords

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

Cite this

Stewart, A.I. ; Clark, I.P. ; Towrie, M. ; Ibrahim, S.K. ; Parker, A.W. ; Pickett, C.J. ; Hunt, Neil T. / Structure and vibrational dynamics of model compounds of the [fefe]-hydrogenase enzyme system via ultrafast two-dimensional infrared spectroscopy. In: Journal of Physical Chemistry B. 2008 ; Vol. 112, No. 32. pp. 10023-10032.
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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.",
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Structure and vibrational dynamics of model compounds of the [fefe]-hydrogenase enzyme system via ultrafast two-dimensional infrared spectroscopy. / Stewart, A.I.; Clark, I.P.; Towrie, M.; Ibrahim, S.K.; Parker, A.W.; Pickett, C.J.; Hunt, Neil T.

In: Journal of Physical Chemistry B, Vol. 112, No. 32, 14.08.2008, p. 10023-10032.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Structure and vibrational dynamics of model compounds of the [fefe]-hydrogenase enzyme system via ultrafast two-dimensional infrared spectroscopy

AU - Stewart, A.I.

AU - Clark, I.P.

AU - Towrie, M.

AU - Ibrahim, S.K.

AU - Parker, A.W.

AU - Pickett, C.J.

AU - Hunt, Neil T.

PY - 2008/8/14

Y1 - 2008/8/14

N2 - 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.

AB - 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.

KW - effective core potentials

KW - 2d ir spectroscopy

KW - echo correlation spectroscopy

KW - effect ohd-oke

KW - molecular calculations

KW - 2d-ir spectroscopy

KW - only hydrogenase

KW - time

KW - transition

KW - evolution

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