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

Claudio Greco, Maurizio Bruschi, Jimmy Heimdal, Piercarlo Fantucci, Luca De Gioia, Ulf Ryde

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskriftPeer review

39 !!Citations (SciVal)

Sammanfattning

[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.
Originalspråkengelska
Sidor (från-till)7256-7258
TidskriftInorganic Chemistry
Volym46
Utgåva18
DOI
StatusPublished - 2007

Bibliografisk information

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)

Ämnesklassifikation (UKÄ)

  • Teoretisk kemi

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