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Catalytic bias and redox-driven inactivation of ancestral FeFe hydrogenases from group B2
Open accessPreprint — published as 10.1021/acscatal.4c01352 · Paper page
Abstract
The biodiversity of hydrogenases, the enzymes that oxidize and produce H 2 , is only just beginning to be explored. Here we use direct electrochemistry to characterize two enzymes from a subgroup of ancestral FeFe hydrogenases, defined by the presence of three adjacent cysteine residues near the active site: the third FeFe hydrogenase from Clostridium pasteurianum (CpIII) and the second from Megasphaera elsdenii (MeII). To examine the functional role of the unusual TSCCCP motif, which defines the group B2 and is replaced with TSCCP in group A hydrogenases, we also produced a CpIII variant where the supernumerary cysteine is deleted. CpIII and MeII inactivate under oxidative conditions in a manner that is distinct from all other previously characterized hydrogenases from group A. Our results suggest that the supernumerary cysteine allows the previously observed sulfide-independent formation of the Hinact state in these enzymes. We also evidence a second reversible, oxidative inactivation process. Because of their inactivation under oxidative conditions, these enzymes are inefficient H 2 oxidation catalysts, but their active site itself is not tuned to make them more active in one particular direction.
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Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Fasano, A., Bailly, A., Wozniak, J., Fourmond, V., & Léger, C.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Léger, Christophe
- Venue
- ACS Catalysis
- Publisher
- openRxiv
- Published
- 2023-06-23
- Volume
- 14
- Issue
- 9
- Pages
- 7001-7010
- ISSN
- 2155-5435 (ISSN-L)
- OpenAlex
- W4394951090
- Cited by
- 22
- References
- 1
- Citations by year
- 2026: 12 · 2025: 7 · 2024: 2 · 2023: 1
- FWCI
- 1.40
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- ACS Catalysis (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- HAL (submittedVersion, cc-by-nc-nd)
- HAL (submittedVersion, other-oa)
- BOA (University of Milano-Bicocca) (submittedVersion)
- Funders
- Aix-Marseille Université (AMX-22-RE-AB-097)
- Agence Nationale de la Recherche (France2030, AMX-22-RE-AB-097, ANR-21-CE50-0041)
- Centre National de la Recherche Scientifique
- Conseil Régional Provence-Alpes-Côte d'Azur
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Electrocatalysts for Energy Conversion
- Keywords
- Clostridium pasteurianum, Megasphaera elsdenii, oxidative inactivation, hydrogenase active site, direct electrochemistry
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