A safety cap protects hydrogenase from oxygen attack

Martin Winkler, Jifu Duan, Andreas Rutz, Christina Felbek, Lisa Scholtysek, Oliver Lampret, Jan Jaenecke, Ulf-Peter Apfel, Gianfranco Gilardi, Francesca Valetti, Vincent Fourmond, Eckhard Hofmann, Christophe Léger () and Thomas Happe ()
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Martin Winkler: Ruhr-Universität Bochum
Jifu Duan: Ruhr-Universität Bochum
Andreas Rutz: Ruhr-Universität Bochum
Christina Felbek: Institut de Microbiologie de la Méditerranée
Lisa Scholtysek: Ruhr-Universität Bochum
Oliver Lampret: Ruhr-Universität Bochum
Jan Jaenecke: Ruhr-Universität Bochum
Ulf-Peter Apfel: Ruhr-Universität Bochum
Gianfranco Gilardi: University of Torino
Francesca Valetti: University of Torino
Vincent Fourmond: Institut de Microbiologie de la Méditerranée
Eckhard Hofmann: Ruhr-Universität Bochum
Christophe Léger: Institut de Microbiologie de la Méditerranée
Thomas Happe: Ruhr-Universität Bochum

Nature Communications, 2021, vol. 12, issue 1, 1-10

Abstract: 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.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-020-20861-2

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DOI: 10.1038/s41467-020-20861-2

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