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A safety cap protects hydrogenase from oxygen attack

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.
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https://hal.archives-ouvertes.fr/hal-03129104
Contributor : Aurélia Bimbi Connect in order to contact the contributor
Submitted on : Wednesday, February 3, 2021 - 3:38:09 PM
Last modification on : Tuesday, October 19, 2021 - 10:50:17 PM

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Distributed under a Creative Commons Attribution 4.0 International License

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Martin Winkler, Jifu Duan, Andreas Rutz, Christina Felbek, Lisa Scholtysek, et al.. A safety cap protects hydrogenase from oxygen attack. Nature Communications, Nature Publishing Group, 2021, 12 (1), ⟨10.1038/s41467-020-20861-2⟩. ⟨hal-03129104⟩

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