Substrate-dependent oxidative inactivation of a W-dependent formate dehydrogenase involving selenocysteine displacement Article Swipe
Guilherme Vilela‐Alves
,
Rita R. Manuel
,
Aldino Viegas
,
Philippe Carpentier
,
Frédéric Biaso
,
Bruno Guigliarelli
,
Inês A. C. Pereira
,
Maria João Romão
,
Cristiano Mota
·
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1101/2024.01.10.571421
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1101/2024.01.10.571421
Metal-dependent formate dehydrogenases are very promising targets for enzyme optimization and design of bio-inspired catalysts for CO 2 reduction, towards novel strategies for climate change mitigation. For effective application of these enzymes, the catalytic mechanism must be fully understood, and the molecular determinants clarified. Despite numerous studies, several doubts persist, namely regarding the role played by the possible dissociation of the SeCys ligand from the Mo/W active site. Additionally, the O 2 sensitivity of these enzymes must also be understood as it poses an important obstacle for biotechnological applications. Here we present a combined biochemical, spectroscopic, and structural characterization of Desulfovibrio vulgaris FdhAB ( Dv FdhAB) when exposed to oxygen in the presence of a substrate (formate or CO 2 ). This study reveals that O 2 inactivation is promoted by the presence of either substrate and involves forming a new species in the active site, captured in the crystal structures, where the SeCys ligand is displaced from tungsten coordination and replaced by a dioxygen or peroxide molecule. This new form was reproducibly obtained and supports the conclusion that, although W- Dv FdhAB can catalyze the oxidation of formate in the presence of oxygen for some minutes, it gets irreversibly inactivated after prolonged O 2 exposure in the presence of either substrate. These results reveal that oxidative inactivation does not require reduction of the metal, as widely assumed, as it can also occur in the oxidized state in the presence of CO 2 .
Related Topics
Concepts
Formate dehydrogenase
Formate
Selenocysteine
Chemistry
Active site
Catalysis
Substrate (aquarium)
Ligand (biochemistry)
Enzyme
Catalase
Combinatorial chemistry
Biochemistry
Biology
Cysteine
Receptor
Ecology
Metadata
- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.1101/2024.01.10.571421
- https://www.biorxiv.org/content/biorxiv/early/2024/01/10/2024.01.10.571421.full.pdf
- OA Status
- green
- References
- 52
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4390744893
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4390744893Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1101/2024.01.10.571421Digital Object Identifier
- Title
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Substrate-dependent oxidative inactivation of a W-dependent formate dehydrogenase involving selenocysteine displacementWork title
- Type
-
preprintOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2024Year of publication
- Publication date
-
2024-01-10Full publication date if available
- Authors
-
Guilherme Vilela‐Alves, Rita R. Manuel, Aldino Viegas, Philippe Carpentier, Frédéric Biaso, Bruno Guigliarelli, Inês A. C. Pereira, Maria João Romão, Cristiano MotaList of authors in order
- Landing page
-
https://doi.org/10.1101/2024.01.10.571421Publisher landing page
- PDF URL
-
https://www.biorxiv.org/content/biorxiv/early/2024/01/10/2024.01.10.571421.full.pdfDirect link to full text PDF
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YesWhether a free full text is available
- OA status
-
greenOpen access status per OpenAlex
- OA URL
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https://www.biorxiv.org/content/biorxiv/early/2024/01/10/2024.01.10.571421.full.pdfDirect OA link when available
- Concepts
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Formate dehydrogenase, Formate, Selenocysteine, Chemistry, Active site, Catalysis, Substrate (aquarium), Ligand (biochemistry), Enzyme, Catalase, Combinatorial chemistry, Biochemistry, Biology, Cysteine, Receptor, EcologyTop concepts (fields/topics) attached by OpenAlex
- Cited by
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0Total citation count in OpenAlex
- References (count)
-
52Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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