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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 Strathclyde researchers, including by researchers from the Physical Activity for Health Group based within the School of Psychological Sciences & Health. Research here seeks to better understand how and why physical activity improves health, gain a better understanding of the amount, intensity, and type of physical activity needed for health benefits, and evaluate the effect of interventions to promote physical activity.

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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.