Stewart, A. Ian and Towrie, M. and Clark, Ian P. and Parker, Anthony W. and Ibrahim, Saad and Pickett, Chris J. and Hunt, Neil T. (2008) PHYS 329-Applications of ultrafast 2-D infrared spectroscopy to studies of the Fe-hydrogenase enzyme system. Abstracts of papers - American Chemical Society, 235. -. ISSN 0065-7727Full text not available in this repository. (Request a copy from the Strathclyde author)
Ultrafast two dimensional infrared spectroscopy has been applied to study the structure and vibrational dynamics of model compounds of the active site of the Fe-hydrogenase enzyme system. 1 Studies of these model systems, which allow separation of the active site of the enzyme from the protein scaffolding allow, by comparison of 2D-IR spectra with density functional theory calculations, determination of the solution phase structure of these species. In addition, vibrational coupling and rapid (<5ps), solvent-mediated equilibration of energy between vibrationally-excited states of the carbonyl ligands of the di-iron-based active site is observed prior to relaxation to the ground state. These dynamics are shown to be solvent-dependent and form a basis for determination of the vibrational interactions between active site and protein. The results of two-colour 2D-IR and 2D-IR studies of transient products of a photo-substitution reaction are also presented, which give new insights into vibrational energy relaxation mechanisms in similar, solution-phase metal-carbonyl systems.
|Keywords:||infrared spectroscopy , enzyme system, Physical and theoretical chemistry, Chemistry(all)|
|Subjects:||Science > Chemistry > Physical and theoretical chemistry|
|Department:||Faculty of Science > Physics|
|Depositing user:||Pure Administrator|
|Date Deposited:||28 Mar 2011 12:22|
|Last modified:||24 May 2016 00:05|