Mechanistic and Physiological Implications of the Interplay among Iron-Sulfur Clusters in [FeFe]-Hydrogenases. A QM/MM Perspective
Greco, Claudio ; Bruschi, Maurizio ; Fantucci, Piercarlo ; Ryde, Ulf LU
and De Gioia, Luca
(2011)
In Journal of the American Chemical Society
133(46).
p.18742-18749
- Abstract
- Key stereoelectronic properties of Desulfovibrio desulfuricans [FeFe]-hydrogenase (DdH) were investigated by quantum mechanical description of its complete inorganic core, which includes a Fe6S6 active site (the H-cluster), as well as two ancillary Fe4S4 assemblies (the F and F' clusters). The partially oxidized, active-ready form of DdH is able to efficiently bind dihydrogen, thus starting H-2 oxidation catalysis. The calculations allow us to unambiguously assign a mixed Fe(H)Fe(I) state to the catalytic core of the active-ready enzyme and show that H-2 uptake exerts subtle, yet crucial influences on the redox properties of DdH. In fact, H-2 binding can promote electron transfer from the H-cluster to the solvent-exposed F'-cluster, thanks... (More)
- Key stereoelectronic properties of Desulfovibrio desulfuricans [FeFe]-hydrogenase (DdH) were investigated by quantum mechanical description of its complete inorganic core, which includes a Fe6S6 active site (the H-cluster), as well as two ancillary Fe4S4 assemblies (the F and F' clusters). The partially oxidized, active-ready form of DdH is able to efficiently bind dihydrogen, thus starting H-2 oxidation catalysis. The calculations allow us to unambiguously assign a mixed Fe(H)Fe(I) state to the catalytic core of the active-ready enzyme and show that H-2 uptake exerts subtle, yet crucial influences on the redox properties of DdH. In fact, H-2 binding can promote electron transfer from the H-cluster to the solvent-exposed F'-cluster, thanks to a 50% decrease of the energy gap between the HOMO (that is localized on the H-cluster) and the LUMO (which is centered on the F'-cluster). Our results also indicate that the binding of the redox partners of DdH in proximity of its F'-cluster can trigger one-electron oxidation of the H-2-bound enzyme, a process that is expected to have an important role in H-2 activation. Our findings are analyzed not only from a mechanistic perspective, but also in consideration of the physiological role of DdH. In fact, this enzyme is known to be able to catalyze both the oxidation and the evolution of H-2, depending on the cellular metabolic requirements. Hints for the design of targeted mutations that could lead to the enhancement of the oxidizing properties of DdH are proposed and discussed. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2272006
- 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
- in
- Journal of the American Chemical Society
- volume
- 133
- issue
- 46
- pages
- 18742 - 18749
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000297398900045
- scopus:83055179384
- pmid:21942468
- ISSN
- 1520-5126
- DOI
- 10.1021/ja205542k
- 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
- d0b99a11-d1ea-4253-ade7-97cc3e13a101 (old id 2272006)
- date added to LUP
- 2016-04-01 14:53:49
- date last changed
- 2023-02-22 07:08:54
@article{d0b99a11-d1ea-4253-ade7-97cc3e13a101,
abstract = {{Key stereoelectronic properties of Desulfovibrio desulfuricans [FeFe]-hydrogenase (DdH) were investigated by quantum mechanical description of its complete inorganic core, which includes a Fe6S6 active site (the H-cluster), as well as two ancillary Fe4S4 assemblies (the F and F' clusters). The partially oxidized, active-ready form of DdH is able to efficiently bind dihydrogen, thus starting H-2 oxidation catalysis. The calculations allow us to unambiguously assign a mixed Fe(H)Fe(I) state to the catalytic core of the active-ready enzyme and show that H-2 uptake exerts subtle, yet crucial influences on the redox properties of DdH. In fact, H-2 binding can promote electron transfer from the H-cluster to the solvent-exposed F'-cluster, thanks to a 50% decrease of the energy gap between the HOMO (that is localized on the H-cluster) and the LUMO (which is centered on the F'-cluster). Our results also indicate that the binding of the redox partners of DdH in proximity of its F'-cluster can trigger one-electron oxidation of the H-2-bound enzyme, a process that is expected to have an important role in H-2 activation. Our findings are analyzed not only from a mechanistic perspective, but also in consideration of the physiological role of DdH. In fact, this enzyme is known to be able to catalyze both the oxidation and the evolution of H-2, depending on the cellular metabolic requirements. Hints for the design of targeted mutations that could lead to the enhancement of the oxidizing properties of DdH are proposed and discussed.}},
author = {{Greco, Claudio and Bruschi, Maurizio and Fantucci, Piercarlo and Ryde, Ulf and De Gioia, Luca}},
issn = {{1520-5126}},
language = {{eng}},
number = {{46}},
pages = {{18742--18749}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Journal of the American Chemical Society}},
title = {{Mechanistic and Physiological Implications of the Interplay among Iron-Sulfur Clusters in [FeFe]-Hydrogenases. A QM/MM Perspective}},
url = {{https://lup.lub.lu.se/search/files/4228341/2338993.pdf}},
doi = {{10.1021/ja205542k}},
volume = {{133}},
year = {{2011}},
}