Probing the effect of the solution environment on the vibrational dynamics of an enzyme model system with ultrafast 2D-IR spectroscopy

G. M. Bonner; A. R. Ridley; S. K. Ibrahim; C. J. Pickett; N. T. Hunt

doi:10.1039/B906163K

Probing the effect of the solution environment on the vibrational dynamics of an enzyme model system with ultrafast 2D-IR spectroscopy

G. M. Bonner, A. R. Ridley, S. K. Ibrahim, C. J. Pickett, N. T. Hunt

Research output: Contribution to journal › Article › peer-review

30 Citations (Scopus)

Abstract

Ultrafast 2D-IRspectroscopy has been applied to study the structure and vibrational dynamics of (µ-C(CH₃)(CH₂S)₂(CH₂S(CH₂)₂Ph)Fe₂(CO)₅, an organometallic model of the active site of the FeFe[hydrogenase] enzyme. 2D-IRspectra have been obtained in solvents ranging from non-polar to polar and protic. The influence of the solvent bath on vibrational relaxation, including rapid intramolecular population transfer, has been characterized. In addition, the temporal dependence of the 2D-IR lineshape has been used to extract information relating to hydrogen bond-mediated spectral diffusion via the frequency–frequency correlation function. Comparisons with previous 2D-IR studies of hydrogenase model systems offer insights into the dependence of the rate of population transfer upon vibrational mode separation and solvent environment, with important implications for the composition and reactivity of the active site of the enzyme.

Original language	English
Pages (from-to)	429-442
Number of pages	14
Journal	Faraday Discussions
Volume	145
DOIs	https://doi.org/10.1039/B906163K
Publication status	Published - 2010

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10.1039/B906163K

Cite this

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title = "Probing the effect of the solution environment on the vibrational dynamics of an enzyme model system with ultrafast 2D-IR spectroscopy",

abstract = "Ultrafast 2D-IRspectroscopy has been applied to study the structure and vibrational dynamics of (µ-C(CH3)(CH2S)2(CH2S(CH2)2Ph)Fe2(CO)5, an organometallic model of the active site of the FeFe[hydrogenase] enzyme. 2D-IRspectra have been obtained in solvents ranging from non-polar to polar and protic. The influence of the solvent bath on vibrational relaxation, including rapid intramolecular population transfer, has been characterized. In addition, the temporal dependence of the 2D-IR lineshape has been used to extract information relating to hydrogen bond-mediated spectral diffusion via the frequency–frequency correlation function. Comparisons with previous 2D-IR studies of hydrogenase model systems offer insights into the dependence of the rate of population transfer upon vibrational mode separation and solvent environment, with important implications for the composition and reactivity of the active site of the enzyme.",

author = "Bonner, {G. M.} and Ridley, {A. R.} and Ibrahim, {S. K.} and Pickett, {C. J.} and Hunt, {N. T.}",

year = "2010",

doi = "10.1039/B906163K",

language = "English",

volume = "145",

pages = "429--442",

journal = "Faraday Discussions",

issn = "1364-5498",

publisher = "Royal Society of Chemistry",

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T1 - Probing the effect of the solution environment on the vibrational dynamics of an enzyme model system with ultrafast 2D-IR spectroscopy

AU - Bonner, G. M.

AU - Ridley, A. R.

AU - Ibrahim, S. K.

AU - Pickett, C. J.

AU - Hunt, N. T.

PY - 2010

Y1 - 2010

N2 - Ultrafast 2D-IRspectroscopy has been applied to study the structure and vibrational dynamics of (µ-C(CH3)(CH2S)2(CH2S(CH2)2Ph)Fe2(CO)5, an organometallic model of the active site of the FeFe[hydrogenase] enzyme. 2D-IRspectra have been obtained in solvents ranging from non-polar to polar and protic. The influence of the solvent bath on vibrational relaxation, including rapid intramolecular population transfer, has been characterized. In addition, the temporal dependence of the 2D-IR lineshape has been used to extract information relating to hydrogen bond-mediated spectral diffusion via the frequency–frequency correlation function. Comparisons with previous 2D-IR studies of hydrogenase model systems offer insights into the dependence of the rate of population transfer upon vibrational mode separation and solvent environment, with important implications for the composition and reactivity of the active site of the enzyme.

AB - Ultrafast 2D-IRspectroscopy has been applied to study the structure and vibrational dynamics of (µ-C(CH3)(CH2S)2(CH2S(CH2)2Ph)Fe2(CO)5, an organometallic model of the active site of the FeFe[hydrogenase] enzyme. 2D-IRspectra have been obtained in solvents ranging from non-polar to polar and protic. The influence of the solvent bath on vibrational relaxation, including rapid intramolecular population transfer, has been characterized. In addition, the temporal dependence of the 2D-IR lineshape has been used to extract information relating to hydrogen bond-mediated spectral diffusion via the frequency–frequency correlation function. Comparisons with previous 2D-IR studies of hydrogenase model systems offer insights into the dependence of the rate of population transfer upon vibrational mode separation and solvent environment, with important implications for the composition and reactivity of the active site of the enzyme.

U2 - 10.1039/B906163K

DO - 10.1039/B906163K

M3 - Article

VL - 145

SP - 429

EP - 442

JO - Faraday Discussions

JF - Faraday Discussions

SN - 1364-5498

ER -