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

Multiple-timescale photoreactivity of a model compound related to the active site of [fefe]-hydrogenase

Ridley, A.R. and Stewart, A. and Adamczyk, K. and Ghosh, H.N. and Kerkeni, B. and Guo, Z.X. and Nibbering, E.T.J. and Pickett, C.J. and Hunt, Neil T. (2008) Multiple-timescale photoreactivity of a model compound related to the active site of [fefe]-hydrogenase. Inorganic Chemistry, 47 (17). pp. 7453-7455. ISSN 0020-1669

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

Abstract

Ultraviolet (UV) photolysis of (mu-S(CH2)(3)S)Fe-2(CO)(6) (1), a model compound of the Fe-hydrogenase enzyme system, has been carried out. When ultrafast UV-pump infrared (IR)-probe spectroscopy, steady-state Fourier transform IR spectroscopic methods, and density functional theory simulations are employed, it has been determined that irradiation of I in an alkane solution at 350 nm leads to the formation of two isomers of the 16-electron complex (mu-S(CH2)(3)S)Fe-2(CO)(5) within 50 ps with evidence of a weakly associated solvent adduct complex. 1 is subsequently recovered on timescales covering several minutes. These studies constitute the first attempt to study the photochemistry and reactivity of these enzyme active site models in solution following carbonyl ligand photolysis.

Item type: Article
ID code: 16766
Keywords: fe-only hydrogenase, clostridium-pasteurianum, Chemistry, Physical and Theoretical Chemistry, Inorganic Chemistry
Subjects: Science > Chemistry
Department: Faculty of Science > Physics
Related URLs:
    Depositing user: Strathprints Administrator
    Date Deposited: 18 Mar 2010 15:18
    Last modified: 05 Sep 2014 02:38
    URI: http://strathprints.strath.ac.uk/id/eprint/16766

    Actions (login required)

    View Item