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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 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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author
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 & Sons
external identifiers
  • wos:000297693200033
  • scopus:82955173089
ISSN
1439-7641
DOI
10.1002/cphc.201100498
language
English
LU publication?
yes
id
cf41b72a-3575-47c8-b2b7-6fcdfd58c797 (old id 2279326)
date added to LUP
2012-01-11 15:23:42
date last changed
2017-02-19 03:19:52
@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},
  keyword      = {bioinorganic chemistry,density functional calculations,electronic,structures,enzyme catalysis,metalloenzymes},
  language     = {eng},
  number       = {17},
  pages        = {3376--3382},
  publisher    = {John Wiley & 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},
  volume       = {12},
  year         = {2011},
}