Strathprints Home | Open Access | Browse | Search | User area | Copyright | Help | Library Home | SUPrimo

PHYS 329-Applications of ultrafast 2-D infrared spectroscopy to studies of the Fe-hydrogenase enzyme system

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 0065-7727

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

Abstract

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.

Item type: Article
ID code: 28974
Keywords: infrared spectroscopy , enzyme system, Physical and theoretical chemistry, Chemistry(all)
Subjects: Science > Chemistry > Physical and theoretical chemistry
Department: Faculty of Science > Physics
Related URLs:
Depositing user: Pure Administrator
Date Deposited: 28 Mar 2011 13:22
Last modified: 27 Mar 2014 09:13
URI: http://strathprints.strath.ac.uk/id/eprint/28974

Actions (login required)

View Item