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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.
Original language | English |
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Pages (from-to) | 15370-15379 |
Number of pages | 10 |
Journal | Journal of Physical Chemistry B |
Volume | 114 |
Issue number | 46 |
DOIs | |
Publication status | Published - 25 Nov 2010 |
Keywords
- effective core potentials
- iron-only hydrogenase
- molecular calculations
- infrared-spectroscopy
- active-site
- subsitute
- spectra
- systems
- bonds
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Dive into the research topics of 'Femtosecond to microsecond photochemistry of a [FeFe]hydrogenase enzyme model compound'. Together they form a unique fingerprint.Projects
- 1 Finished
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TWO DIMENSIONAL INFRARED SPECTROSCOPY - A NEW APPROACH TO UNDERSTANDING ENZYME CHEMISTRY
Hunt, N. (Fellow)
EPSRC (Engineering and Physical Sciences Research Council)
1/10/06 → 30/09/11
Project: Research Fellowship