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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2279326
- author
- Greco, Claudio
; Bruschi, Maurizio
; Fantucci, Piercarlo
; Ryde, Ulf
LU
and De Gioia, Luca
- organization
- publishing date
- 2011
- 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 Inc.
- 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
- 2023-01-02 18:01:21
@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}},
keywords = {{bioinorganic chemistry; density functional calculations; electronic; structures; enzyme catalysis; metalloenzymes}},
language = {{eng}},
number = {{17}},
pages = {{3376--3382}},
publisher = {{John Wiley & Sons Inc.}},
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}},
}