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

Spyridon Kaziannis, Joseph A. Wright, Marco Candelaresi, Rafal Kania, Gregory M. Greetham, Anthony W. Parker, Christopher J. Pickett, Neil T. Hunt

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The vibrational dynamics of (mu-propanedithiolate)Fe-2(CO)(4)(CN)(2)(2-), 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.

Original languageEnglish
Pages (from-to)10295-10305
Number of pages11
JournalPhysical Chemistry Chemical Physics
Volume13
Issue number21
Early online date3 May 2011
DOIs
Publication statusPublished - 2011

Keywords

  • 2-dimensional infrared-spectroscopy
  • FE-only hydrogenases
  • 2d ir spectroscopy
  • molecular calculations
  • active-site
  • subsite
  • potentials
  • equilibrium
  • elements
  • desulfovibrio-desulfuricans
  • TIC - Bionanotechnology

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