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

Kaziannis, Spyridon, Santabarbara, Stefano, Wright, Joseph A ORCID: https://orcid.org/0000-0001-9603-1001, Greetham, Gregory M., Towrie, Michael, Parker, Anthony W., Pickett, Christopher J and Hunt, Neil (2010) Femtosecond to microsecond photochemistry of a [FeFe]hydrogenase enzyme model compound. The Journal of Physical Chemistry B, 114 (46). pp. 15370-15379. ISSN 1520-5207

Full text not available from this repository.

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.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Synthetic Chemistry (former - to 2017) Faculty of Science > Research Groups > Chemistry of Materials and Catalysis Faculty of Science > Research Groups > Chemistry of Light and Energy Faculty of Science > Research Groups > Energy Materials Laboratory
Depositing User:	Rachel Smith
Date Deposited:	23 Mar 2011 16:11
Last Modified:	24 Sep 2024 09:08
URI:	https://ueaeprints.uea.ac.uk/id/eprint/27070
DOI:	10.1021/jp107618n

Actions (login required)

View Item