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Targeting Intermediates of [FeFe]-Hydrogenase by CO and CN Vibrational Signatures

Yu, Lian; Greco, Claudio; Bruschi, Maurizio; Ryde, Ulf LU ; De Gioia, Luca and Reiheet, Markus (2011) In Inorganic Chemistry 50(9). p.3888-3900
Abstract
In this work, we employ density functional theory to assign vibrational signatures of [FeFe]-hydrogenase intermediates to molecular structures. For this purpose, we perform an exhaustive analysis of structures and harmonic vibrations of a series of CN and CO containing model clusters of the [FeFe]-hydrogenase enzyme active site considering also different charges, counterions, and solvents. The pure density functional BP86 in combination with a triple-xi polarized basis set produce reliable molecular structures as well as harmonic vibrations. Calculated CN and CO stretching vibrations are analyzed separately. Scaled vibrational frequencies are then applied to assign intermediates,in [FeFe]-hydrogenase's reaction cycle. The. " results nicely... (More)
In this work, we employ density functional theory to assign vibrational signatures of [FeFe]-hydrogenase intermediates to molecular structures. For this purpose, we perform an exhaustive analysis of structures and harmonic vibrations of a series of CN and CO containing model clusters of the [FeFe]-hydrogenase enzyme active site considering also different charges, counterions, and solvents. The pure density functional BP86 in combination with a triple-xi polarized basis set produce reliable molecular structures as well as harmonic vibrations. Calculated CN and CO stretching vibrations are analyzed separately. Scaled vibrational frequencies are then applied to assign intermediates,in [FeFe]-hydrogenase's reaction cycle. The. " results nicely complement the previous studies of Darensbourg and The infrared spectrum of the H-ox form is in very good agreement with the calculated Spectrum of the (FeFeII)-Fe-I-model complex featuring a free coordination site at the distal Fe atom, as well as, With the calculated spectra of the complexes in which H-2 or H2O are coordinated at this site The spectrum of H-red measured from Desulfovibrio desulfuricans is compatible with a mixture of a (FeFeI)-Fe-I species with all terminal COs, and a (FeFeI)-Fe-I species with protonated dtma ligand, while the spectrum of H-red recently measured from Chlamydomonas reinhardtii is compatible with a mixture of a (FeFeI)-Fe-I species with a bridged CO, and a (FeFeII)-Fe-II species with a terminal hydride bound to the Fe atom. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Inorganic Chemistry
volume
50
issue
9
pages
3888 - 3900
publisher
The American Chemical Society
external identifiers
  • wos:000289710700007
  • scopus:79955372778
ISSN
1520-510X
DOI
10.1021/ic102039z
language
English
LU publication?
yes
id
1e85f47c-93d6-42f5-9b5b-b2243265c2a0 (old id 1964988)
date added to LUP
2011-05-23 12:02:08
date last changed
2017-09-24 03:07:05
@article{1e85f47c-93d6-42f5-9b5b-b2243265c2a0,
  abstract     = {In this work, we employ density functional theory to assign vibrational signatures of [FeFe]-hydrogenase intermediates to molecular structures. For this purpose, we perform an exhaustive analysis of structures and harmonic vibrations of a series of CN and CO containing model clusters of the [FeFe]-hydrogenase enzyme active site considering also different charges, counterions, and solvents. The pure density functional BP86 in combination with a triple-xi polarized basis set produce reliable molecular structures as well as harmonic vibrations. Calculated CN and CO stretching vibrations are analyzed separately. Scaled vibrational frequencies are then applied to assign intermediates,in [FeFe]-hydrogenase's reaction cycle. The. " results nicely complement the previous studies of Darensbourg and The infrared spectrum of the H-ox form is in very good agreement with the calculated Spectrum of the (FeFeII)-Fe-I-model complex featuring a free coordination site at the distal Fe atom, as well as, With the calculated spectra of the complexes in which H-2 or H2O are coordinated at this site The spectrum of H-red measured from Desulfovibrio desulfuricans is compatible with a mixture of a (FeFeI)-Fe-I species with all terminal COs, and a (FeFeI)-Fe-I species with protonated dtma ligand, while the spectrum of H-red recently measured from Chlamydomonas reinhardtii is compatible with a mixture of a (FeFeI)-Fe-I species with a bridged CO, and a (FeFeII)-Fe-II species with a terminal hydride bound to the Fe atom.},
  author       = {Yu, Lian and Greco, Claudio and Bruschi, Maurizio and Ryde, Ulf and De Gioia, Luca and Reiheet, Markus},
  issn         = {1520-510X},
  language     = {eng},
  number       = {9},
  pages        = {3888--3900},
  publisher    = {The American Chemical Society},
  series       = {Inorganic Chemistry},
  title        = {Targeting Intermediates of [FeFe]-Hydrogenase by CO and CN Vibrational Signatures},
  url          = {http://dx.doi.org/10.1021/ic102039z},
  volume       = {50},
  year         = {2011},
}