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Structural insights into the active-ready form of [FeFe]-Hydrogenase and mechanistic details of its inhibition by carbon monoxide

Greco, Claudio LU ; Bruschi, Maurizio ; Heimdal, Jimmy LU ; Fantucci, Piercarlo ; De Gioia, Luca and Ryde, Ulf LU orcid (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)
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author
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organization
publishing date
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}},
}