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Probing the Effects of One-Electron Reduction and Protonation on the Electronic Properties of the Fe-S Clusters in the Active-Ready Form of [FeFe]-Hydrogenases. A QM/MM Investigation.

Greco, Claudio ; Bruschi, Maurizio ; Fantucci, Piercarlo ; Ryde, Ulf LU orcid and De Gioia, Luca (2011) In ChemPhysChem 12(17). p.3376-3382
Abstract
A QM/MM investigation of the active-ready (Hox) form of [FeFe]-hydrogenase from D. desulfuricans, in which the electronic properties of all Fe-S clusters (H, F and F') have been simultaneously described using DFT, was carried out with the aim of disclosing a possible interplay between the H-cluster and the accessory iron-sulfur clusters in the initial steps of the catalytic process leading to H2 formation. It turned out that one-electron addition to the active-ready form leads to reduction of the F'-cluster and not of the H-cluster. Protonation of the H-cluster in Hox is unlikely, and in any case it would not trigger electron transfer from the accessory Fe4S4 clusters to the active site. Instead, one-electron reduction and protonation of... (More)
A QM/MM investigation of the active-ready (Hox) form of [FeFe]-hydrogenase from D. desulfuricans, in which the electronic properties of all Fe-S clusters (H, F and F') have been simultaneously described using DFT, was carried out with the aim of disclosing a possible interplay between the H-cluster and the accessory iron-sulfur clusters in the initial steps of the catalytic process leading to H2 formation. It turned out that one-electron addition to the active-ready form leads to reduction of the F'-cluster and not of the H-cluster. Protonation of the H-cluster in Hox is unlikely, and in any case it would not trigger electron transfer from the accessory Fe4S4 clusters to the active site. Instead, one-electron reduction and protonation of the active-ready form trigger electron transfer within the protein, a key event in the catalytic cycle. In particular, protonation of the H-cluster after one-electron reduction of the enzyme lowers the energy of the lowest unoccupied molecular orbitals localized on the H-cluster to such an extent that a long-range electron transfer from the F'-cluster towards the H-cluster itself is allowed. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
bioinorganic chemistry, density functional calculations, electronic, structures, enzyme catalysis, metalloenzymes
in
ChemPhysChem
volume
12
issue
17
pages
3376 - 3382
publisher
John Wiley and Sons
external identifiers
  • wos:000297693200033
  • scopus:82955173089
  • pmid:22084023
ISSN
1439-7641
DOI
10.1002/cphc.201100498
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
cf41b72a-3575-47c8-b2b7-6fcdfd58c797 (old id 2279326)
date added to LUP
2016-04-01 11:00:48
date last changed
2021-01-06 02:46:32
@article{cf41b72a-3575-47c8-b2b7-6fcdfd58c797,
  abstract     = {A QM/MM investigation of the active-ready (Hox) form of [FeFe]-hydrogenase from D. desulfuricans, in which the electronic properties of all Fe-S clusters (H, F and F') have been simultaneously described using DFT, was carried out with the aim of disclosing a possible interplay between the H-cluster and the accessory iron-sulfur clusters in the initial steps of the catalytic process leading to H2 formation. It turned out that one-electron addition to the active-ready form leads to reduction of the F'-cluster and not of the H-cluster. Protonation of the H-cluster in Hox is unlikely, and in any case it would not trigger electron transfer from the accessory Fe4S4 clusters to the active site. Instead, one-electron reduction and protonation of the active-ready form trigger electron transfer within the protein, a key event in the catalytic cycle. In particular, protonation of the H-cluster after one-electron reduction of the enzyme lowers the energy of the lowest unoccupied molecular orbitals localized on the H-cluster to such an extent that a long-range electron transfer from the F'-cluster towards the H-cluster itself is allowed.},
  author       = {Greco, Claudio and Bruschi, Maurizio and Fantucci, Piercarlo and Ryde, Ulf and De Gioia, Luca},
  issn         = {1439-7641},
  language     = {eng},
  number       = {17},
  pages        = {3376--3382},
  publisher    = {John Wiley and Sons},
  series       = {ChemPhysChem},
  title        = {Probing the Effects of One-Electron Reduction and Protonation on the Electronic Properties of the Fe-S Clusters in the Active-Ready Form of [FeFe]-Hydrogenases. A QM/MM Investigation.},
  url          = {http://dx.doi.org/10.1002/cphc.201100498},
  doi          = {10.1002/cphc.201100498},
  volume       = {12},
  year         = {2011},
}