Picture of wind turbine against blue sky

Open Access research with a real impact...

The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs.

The Energy Systems Research Unit (ESRU) within Strathclyde's Department of Mechanical and Aerospace Engineering is producing Open Access research that can help society deploy and optimise renewable energy systems, such as wind turbine technology.

Explore wind turbine research in Strathprints

Explore all of Strathclyde's Open Access research content

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

Bonner, G. M. and Ridley, A. R. and Ibrahim, S. K. and Pickett, C. J. and Hunt, N. T. (2010) Probing the effect of the solution environment on the vibrational dynamics of an enzyme model system with ultrafast 2D-IR spectroscopy. Faraday Discussions, 145. pp. 429-442. ISSN 1359-6640

Full text not available in this repository. (Request a copy from the Strathclyde author)

Abstract

Ultrafast 2D-IR spectroscopy has been applied to study the structure and vibrational dynamics of (mu-C(CH3)(CH2S)(2)(CH2S(CH2)(2)Ph)Fe-2(CO)(5), an organometallic model of the active site of the FeFe[hydrogenase] enzyme. 2D-IR spectra 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.