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The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of Open Access research papers by University of Strathclyde researchers, including by researchers from the Department of Computer & Information Sciences involved in mathematically structured programming, similarity and metric search, computer security, software systems, combinatronics and digital health.

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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

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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.