Structural insights into the active-ready form of [FeFe]-Hydrogenase and mechanistic details of its inhibition by carbon monoxide
(2007) In Inorganic Chemistry 46(18). p.7256-7258- Abstract
- [FeFe]-Hydrogenases harbor a {2Fe3S} assembly bearing two CO and two CN- groups, a mu-CO ligand, and a vacant coordination site trans to the mu-CO group. Recent theoretical results obtained studying the isolated {2Fe3S} subsite indicated that one of the CN- ligands can easily move from the crystallographic position to the coordination site trans to the mu-CO group; such an isomerization would have a major impact on substrates and inhibitors binding regiochemistry and, consequently, on the catalytic mechanism. To shed light on this crucial issue, we have carried out hybrid QM/MM and free energy perturbation calculations on the whole enzyme, which demonstrate that the protein environment plays a crucial role and maintains the CN- group fixed... (More)
- [FeFe]-Hydrogenases harbor a {2Fe3S} assembly bearing two CO and two CN- groups, a mu-CO ligand, and a vacant coordination site trans to the mu-CO group. Recent theoretical results obtained studying the isolated {2Fe3S} subsite indicated that one of the CN- ligands can easily move from the crystallographic position to the coordination site trans to the mu-CO group; such an isomerization would have a major impact on substrates and inhibitors binding regiochemistry and, consequently, on the catalytic mechanism. To shed light on this crucial issue, we have carried out hybrid QM/MM and free energy perturbation calculations on the whole enzyme, which demonstrate that the protein environment plays a crucial role and maintains the CN- group fixed in the position observed in the crystal structure; these results strongly support the hypothesis that the vacant coordination site trans to the mu-CO group has a crucial functional relevance both in the context of CO-mediated inhibition of the enzyme and in dihydrogen oxidation/evolution catalysis. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/688036
- author
- Greco, Claudio
LU
; Bruschi, Maurizio
; Heimdal, Jimmy
LU
; Fantucci, Piercarlo
; De Gioia, Luca
and Ryde, Ulf
LU
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Inorganic Chemistry
- volume
- 46
- issue
- 18
- pages
- 7256 - 7258
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000248984500011
- scopus:34548635010
- ISSN
- 1520-510X
- DOI
- 10.1021/ic701051h
- 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
- 8c4d4af8-d7bb-4f24-9b84-c05586d94a5e (old id 688036)
- date added to LUP
- 2016-04-01 11:59:39
- date last changed
- 2023-01-03 02:20:08
@article{8c4d4af8-d7bb-4f24-9b84-c05586d94a5e, abstract = {{[FeFe]-Hydrogenases harbor a {2Fe3S} assembly bearing two CO and two CN- groups, a mu-CO ligand, and a vacant coordination site trans to the mu-CO group. Recent theoretical results obtained studying the isolated {2Fe3S} subsite indicated that one of the CN- ligands can easily move from the crystallographic position to the coordination site trans to the mu-CO group; such an isomerization would have a major impact on substrates and inhibitors binding regiochemistry and, consequently, on the catalytic mechanism. To shed light on this crucial issue, we have carried out hybrid QM/MM and free energy perturbation calculations on the whole enzyme, which demonstrate that the protein environment plays a crucial role and maintains the CN- group fixed in the position observed in the crystal structure; these results strongly support the hypothesis that the vacant coordination site trans to the mu-CO group has a crucial functional relevance both in the context of CO-mediated inhibition of the enzyme and in dihydrogen oxidation/evolution catalysis.}}, author = {{Greco, Claudio and Bruschi, Maurizio and Heimdal, Jimmy and Fantucci, Piercarlo and De Gioia, Luca and Ryde, Ulf}}, issn = {{1520-510X}}, language = {{eng}}, number = {{18}}, pages = {{7256--7258}}, publisher = {{The American Chemical Society (ACS)}}, series = {{Inorganic Chemistry}}, title = {{Structural insights into the active-ready form of [FeFe]-Hydrogenase and mechanistic details of its inhibition by carbon monoxide}}, url = {{http://dx.doi.org/10.1021/ic701051h}}, doi = {{10.1021/ic701051h}}, volume = {{46}}, year = {{2007}}, }