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The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs.

Strathprints serves world leading Open Access research by the University of Strathclyde, including research by the Strathclyde Institute of Pharmacy and Biomedical Sciences (SIPBS), where research centres such as the Industrial Biotechnology Innovation Centre (IBioIC), the Cancer Research UK Formulation Unit, SeaBioTech and the Centre for Biophotonics are based.

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Femtosecond to microsecond photochemistry of a [FeFe]hydrogenase enzyme model compound

Kaziannis, Spyridon and Santabarbara, Stefano and Wright, Joseph A. and Greetham, Gregory M. and Towrie, Michael and Parker, Anthony W. and Pickett, Christopher J. and Hunt, Neil T. (2010) Femtosecond to microsecond photochemistry of a [FeFe]hydrogenase enzyme model compound. Journal of Physical Chemistry B, 114 (46). pp. 15370-15379. ISSN 1520-6106

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Abstract

The photochemistry and dynamics of a model compound of the active site of the [FeFe]hydrogenase enzyme system have been studied on a wide range of time scales using a unique combination of femtosecond time-resolved infrared spectroscopy, nanosecond time-resolved infrared spectroscopy, and steady-state UV-FTIR methods. Using three different solvents, heptane, acetonitrile, and cyanoheptane, we have observed the rapid formation of solvent adduct species from the first solvation shell of the solute following photolysis of a carbonyl ligand and global fitting techniques have been employed to provide new insights into the ultrafast dynamics of this process. In addition, the use of solvent mixtures has enabled the observation of competitive ligand substitution processes at the newly created coordination site on time scales of a few nanoseconds, shedding new light on the chemical behavior of these enzyme models.