The role of CN and CO ligands in the vibrational relaxation dynamics of model compounds of the [FeFe]-hydrogenase enzyme

Kaziannis, Spyridon, Wright, Joseph A. ORCID: https://orcid.org/0000-0001-9603-1001, Candelaresi, Marco, Kania, Rafal, Greetham, Gregory M., Parker, Anthony W., Pickett, Christopher J. and Hunt, Neil T. (2011) The role of CN and CO ligands in the vibrational relaxation dynamics of model compounds of the [FeFe]-hydrogenase enzyme. Physical Chemistry Chemical Physics, 13 (21). pp. 10295-10305. ISSN 1463-9076

Full text not available from this repository.

Abstract

The vibrational dynamics of (µ-propanedithiolate)Fe2(CO)4(CN)22-, a model compound of the active site of the [FeFe]-hydrogenase enzyme, have been examined via ultrafast 2D-IR spectroscopy. The results indicate that the vibrational coupling between the stretching modes of the CO and CN ligands is small and restricted to certain modes but the slow growth of off-diagonal peaks is assigned to population transfer processes occurring between these modes on timescales of 30–40 ps. Analysis of the dynamics in concert with anharmonic density functional theory simulations shows that the presence of CN ligands alters the vibrational relaxation dynamics of the CO modes in comparison to all-carbonyl model systems and suggests that the presence of these ligands in the enzyme may be an important feature in terms of directing the vibrational relaxation mechanism.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Chemistry of Materials and Catalysis 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 Light and Energy Faculty of Science > Research Groups > Energy Materials Laboratory
Depositing User:	Rhiannon Harvey
Date Deposited:	21 Mar 2012 16:08
Last Modified:	24 Sep 2024 09:04
URI:	https://ueaeprints.uea.ac.uk/id/eprint/38423
DOI:	10.1039/c1cp20589g

Actions (login required)

View Item