Data di Pubblicazione:
2021
Abstract:
[FeFe]-hydrogenases are efficient H2-catalysts, yet upon contact with dioxygen their catalytic cofactor (H-cluster) is irreversibly inactivated. Here, we combine X-ray crystallography, rational protein design, direct electrochemistry, and Fourier-transform infrared spectroscopy to describe a protein morphing mechanism that controls the reversible transition between the catalytic Hox-state and the inactive but oxygen-resistant Hinact-state in [FeFe]-hydrogenase CbA5H of Clostridium beijerinckii. The X-ray structure of air-exposed CbA5H reveals that a conserved cysteine residue in the local environment of the active site (H-cluster) directly coordinates the substrate-binding site, providing a safety cap that prevents O2-binding and consequently, cofactor degradation. This protection mechanism depends on three non-conserved amino acids situated approximately 13 Å away from the H-cluster, demonstrating that the 1st coordination sphere chemistry of the H-cluster can be remote-controlled by distant residues.
Tipologia CRIS:
03A-Articolo su Rivista
Keywords:
Binding Sites; Catalytic Domain; Clostridium beijerinckii; Crystallography, X-Ray; Electrochemistry; Kinetics; Models, Theoretical; Spectroscopy, Fourier Transform Infrared
Elenco autori:
Winkler M.; Duan J.; Rutz A.; Felbek C.; Scholtysek L.; Lampret O.; Jaenecke J.; Apfel U.-P.; Gilardi G.; Valetti F.; Fourmond V.; Hofmann E.; Leger C.; Happe T.
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