Targeting Intermediates of [FeFe]-Hydrogenase by CO and CN Vibrational Signatures
(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:
https://lup.lub.lu.se/record/1964988
- author
- Yu, Lian ; Greco, Claudio ; Bruschi, Maurizio ; Ryde, Ulf LU ; De Gioia, Luca and Reiheet, Markus
- organization
- publishing date
- 2011
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Inorganic Chemistry
- volume
- 50
- issue
- 9
- pages
- 3888 - 3900
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000289710700007
- scopus:79955372778
- pmid:21443182
- ISSN
- 1520-510X
- DOI
- 10.1021/ic102039z
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)
- id
- 1e85f47c-93d6-42f5-9b5b-b2243265c2a0 (old id 1964988)
- date added to LUP
- 2016-04-01 10:08:26
- date last changed
- 2023-02-02 23:53:36
@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 (ACS)}}, series = {{Inorganic Chemistry}}, title = {{Targeting Intermediates of [FeFe]-Hydrogenase by CO and CN Vibrational Signatures}}, url = {{https://lup.lub.lu.se/search/files/1597157/2338987.pdf}}, doi = {{10.1021/ic102039z}}, volume = {{50}}, year = {{2011}}, }