Functionally Relevant Interplay between the Fe(4)S(4) Cluster and CN(-) Ligands in the Active Site of [FeFe]-Hydrogenases.
Bruschi, Maurizio ; Greco, Claudio ; Bertini, Luca ; Fantucci, Piercarlo ; Ryde, Ulf LU
and Gioia, Luca De
(2010)
In Journal of the American Chemical Society
132(14).
p.4992-4992
- Abstract
- [FeFe]-hydrogenases are highly efficient H(2)-evolving metalloenzymes that include cyanides and carbonyls in the active site. The latter is an Fe(6)S(6) cluster (the so-called H-cluster) that can be subdivided into a binuclear portion carrying the CO and CN(-) groups and a tetranuclear subcluster. The fundamental role of cyanide ligands in increasing the basicity of the H-cluster has been highlighted previously. Here a more subtle but crucial role played by the two CN(-) ligands in the active site of [FeFe]-hydrogenases is disclosed. In fact, QM/MM calculations on all-atom models of the enzyme from Desulfovibrio desulfuricans show that the cyanide groups fine-tune the electronic and redox properties of the active site, affecting both the... (More)
- [FeFe]-hydrogenases are highly efficient H(2)-evolving metalloenzymes that include cyanides and carbonyls in the active site. The latter is an Fe(6)S(6) cluster (the so-called H-cluster) that can be subdivided into a binuclear portion carrying the CO and CN(-) groups and a tetranuclear subcluster. The fundamental role of cyanide ligands in increasing the basicity of the H-cluster has been highlighted previously. Here a more subtle but crucial role played by the two CN(-) ligands in the active site of [FeFe]-hydrogenases is disclosed. In fact, QM/MM calculations on all-atom models of the enzyme from Desulfovibrio desulfuricans show that the cyanide groups fine-tune the electronic and redox properties of the active site, affecting both the protonation regiochemistry and electron transfer between the two subclusters of the H-cluster. Despite the crucial role of cyanides in the protein active site, the currently available bioinspired electrocatalysts generally lack CN(-) groups in order to avoid competition between the latter and the catalytic metal centers for proton binding. In this respect, we show that a targeted inclusion of phosphine ligands in hexanuclear biomimetic clusters may restore the electronic and redox features of the wild-type H-cluster. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1581786
- author
- Bruschi, Maurizio
; Greco, Claudio
; Bertini, Luca
; Fantucci, Piercarlo
; Ryde, Ulf
LU
and Gioia, Luca De
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of the American Chemical Society
- volume
- 132
- issue
- 14
- pages
- 4992 - 4992
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000276553700010
- pmid:20302340
- scopus:77950806359
- pmid:20302340
- ISSN
- 1520-5126
- DOI
- 10.1021/ja1008773
- 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
- afd8b3c3-6907-425a-8bbc-fdc645f69963 (old id 1581786)
- date added to LUP
- 2016-04-01 13:25:57
- date last changed
- 2025-04-04 15:17:38
@article{afd8b3c3-6907-425a-8bbc-fdc645f69963,
abstract = {{[FeFe]-hydrogenases are highly efficient H(2)-evolving metalloenzymes that include cyanides and carbonyls in the active site. The latter is an Fe(6)S(6) cluster (the so-called H-cluster) that can be subdivided into a binuclear portion carrying the CO and CN(-) groups and a tetranuclear subcluster. The fundamental role of cyanide ligands in increasing the basicity of the H-cluster has been highlighted previously. Here a more subtle but crucial role played by the two CN(-) ligands in the active site of [FeFe]-hydrogenases is disclosed. In fact, QM/MM calculations on all-atom models of the enzyme from Desulfovibrio desulfuricans show that the cyanide groups fine-tune the electronic and redox properties of the active site, affecting both the protonation regiochemistry and electron transfer between the two subclusters of the H-cluster. Despite the crucial role of cyanides in the protein active site, the currently available bioinspired electrocatalysts generally lack CN(-) groups in order to avoid competition between the latter and the catalytic metal centers for proton binding. In this respect, we show that a targeted inclusion of phosphine ligands in hexanuclear biomimetic clusters may restore the electronic and redox features of the wild-type H-cluster.}},
author = {{Bruschi, Maurizio and Greco, Claudio and Bertini, Luca and Fantucci, Piercarlo and Ryde, Ulf and Gioia, Luca De}},
issn = {{1520-5126}},
language = {{eng}},
number = {{14}},
pages = {{4992--4992}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Journal of the American Chemical Society}},
title = {{Functionally Relevant Interplay between the Fe(4)S(4) Cluster and CN(-) Ligands in the Active Site of [FeFe]-Hydrogenases.}},
url = {{https://lup.lub.lu.se/search/files/136743360/138_feh2ase_cn_jacs.pdf}},
doi = {{10.1021/ja1008773}},
volume = {{132}},
year = {{2010}},
}