Magnetic Properties of [FeFe]-Hydrogenases: A Theoretical Investigation Based on Extended QM and QM/MM Models of the H-Cluster and Its Surroundings
(2011) In European Journal of Inorganic Chemistry p.1043-1049- Abstract
- In the present contribution, we report a theoretical investigation of the magnetic properties of the dihydrogen-evolving enzyme [FeFe]-hydrogenase, based on both DFT models of the active site (the H-cluster, a Fe6S6 assembly including a binuclear portion directly involved in substrates binding), and QM/MM models of the whole enzyme. Antiferromagnetic coupling within the H-cluster has been treated using the broken-symmetry approach, along with the use of different density functionals. Results of g value calculations turned out to vary as a function of the level of theory and of the extension of the model. The choice of the broken-symmetry coupling scheme also had a significant influence on the calculated g values, for both the active-ready... (More)
- In the present contribution, we report a theoretical investigation of the magnetic properties of the dihydrogen-evolving enzyme [FeFe]-hydrogenase, based on both DFT models of the active site (the H-cluster, a Fe6S6 assembly including a binuclear portion directly involved in substrates binding), and QM/MM models of the whole enzyme. Antiferromagnetic coupling within the H-cluster has been treated using the broken-symmetry approach, along with the use of different density functionals. Results of g value calculations turned out to vary as a function of the level of theory and of the extension of the model. The choice of the broken-symmetry coupling scheme also had a significant influence on the calculated g values, for both the active-ready (H-ox) and the CO-inhibited (H-ox-CO) enzyme forms. However, hyper-fine coupling-constant calculations were found to provide more consistent results. This allowed us to show that the experimentally detected delocalization of an unpaired electron at the binuclear subcluster in Desulfovibrio desulfuricans Hox is compatible with a weak interaction between the catalytic centre and a low-weight exogenous ligand like a water molecule. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1868502
- author
- Greco, Claudio ; Silakov, Alexey ; Bruschi, Maurizio ; Ryde, Ulf LU ; De Gioia, Luca and Lubitz, Wolfgang
- organization
- publishing date
- 2011
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Computer chemistry, Density functional calculations, Magnetic, properties, EPR parameters calculation, Quantum mechanics, Enzymes, Hydrogenases, Hydrogen
- in
- European Journal of Inorganic Chemistry
- issue
- 7
- pages
- 1043 - 1049
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000288099000015
- scopus:79951872903
- ISSN
- 1099-0682
- DOI
- 10.1002/ejic.201001058
- 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
- 09a0d005-0e6e-4a34-a78f-1c3004f6a669 (old id 1868502)
- date added to LUP
- 2016-04-01 09:53:50
- date last changed
- 2023-02-07 02:35:24
@article{09a0d005-0e6e-4a34-a78f-1c3004f6a669, abstract = {{In the present contribution, we report a theoretical investigation of the magnetic properties of the dihydrogen-evolving enzyme [FeFe]-hydrogenase, based on both DFT models of the active site (the H-cluster, a Fe6S6 assembly including a binuclear portion directly involved in substrates binding), and QM/MM models of the whole enzyme. Antiferromagnetic coupling within the H-cluster has been treated using the broken-symmetry approach, along with the use of different density functionals. Results of g value calculations turned out to vary as a function of the level of theory and of the extension of the model. The choice of the broken-symmetry coupling scheme also had a significant influence on the calculated g values, for both the active-ready (H-ox) and the CO-inhibited (H-ox-CO) enzyme forms. However, hyper-fine coupling-constant calculations were found to provide more consistent results. This allowed us to show that the experimentally detected delocalization of an unpaired electron at the binuclear subcluster in Desulfovibrio desulfuricans Hox is compatible with a weak interaction between the catalytic centre and a low-weight exogenous ligand like a water molecule.}}, author = {{Greco, Claudio and Silakov, Alexey and Bruschi, Maurizio and Ryde, Ulf and De Gioia, Luca and Lubitz, Wolfgang}}, issn = {{1099-0682}}, keywords = {{Computer chemistry; Density functional calculations; Magnetic; properties; EPR parameters calculation; Quantum mechanics; Enzymes; Hydrogenases; Hydrogen}}, language = {{eng}}, number = {{7}}, pages = {{1043--1049}}, publisher = {{John Wiley & Sons Inc.}}, series = {{European Journal of Inorganic Chemistry}}, title = {{Magnetic Properties of [FeFe]-Hydrogenases: A Theoretical Investigation Based on Extended QM and QM/MM Models of the H-Cluster and Its Surroundings}}, url = {{https://lup.lub.lu.se/search/files/136742673/152_feh2ase_epr.pdf}}, doi = {{10.1002/ejic.201001058}}, year = {{2011}}, }