Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme Reoxidation
Metal-dependent formate dehydrogenases (Fdh) catalyze the reversible conversion of CO<sub>2</sub> to formate, with unrivalled efficiency and selectivity. However, the key catalytic aspects of these enzymes remain unknown, preventing us from fully benefiting from their capabilities in ter...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-12-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/1/476 |
| _version_ | 1797625649349787648 |
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| author | Guilherme Vilela-Alves Rita Rebelo Manuel Ana Rita Oliveira Inês Cardoso Pereira Maria João Romão Cristiano Mota |
| author_facet | Guilherme Vilela-Alves Rita Rebelo Manuel Ana Rita Oliveira Inês Cardoso Pereira Maria João Romão Cristiano Mota |
| author_sort | Guilherme Vilela-Alves |
| collection | DOAJ |
| description | Metal-dependent formate dehydrogenases (Fdh) catalyze the reversible conversion of CO<sub>2</sub> to formate, with unrivalled efficiency and selectivity. However, the key catalytic aspects of these enzymes remain unknown, preventing us from fully benefiting from their capabilities in terms of biotechnological applications. Here, we report a time-resolved characterization by X-ray crystallography of the <i>Desulfovibrio vulgaris</i> Hildenborough SeCys/W-Fdh during formate oxidation. The results allowed us to model five different intermediate structures and to chronologically map the changes occurring during enzyme reduction. Formate molecules were assigned for the first time to populate the catalytic pocket of a Fdh. Finally, the redox reversibility of <i>Dv</i>FdhAB in crystals was confirmed by reduction and reoxidation structural studies. |
| first_indexed | 2024-03-11T09:59:17Z |
| format | Article |
| id | doaj.art-d7c29ddc7f9748668efe496682f04a15 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T09:59:17Z |
| publishDate | 2022-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-d7c29ddc7f9748668efe496682f04a152023-11-16T15:33:56ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-12-0124147610.3390/ijms24010476Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme ReoxidationGuilherme Vilela-Alves0Rita Rebelo Manuel1Ana Rita Oliveira2Inês Cardoso Pereira3Maria João Romão4Cristiano Mota5Associate Laboratory i4HB—Institute for Health and Bioeconomy, NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829-516 Caparica, PortugalInstituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, 2780-157 Oeiras, PortugalInstituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, 2780-157 Oeiras, PortugalInstituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, 2780-157 Oeiras, PortugalAssociate Laboratory i4HB—Institute for Health and Bioeconomy, NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829-516 Caparica, PortugalAssociate Laboratory i4HB—Institute for Health and Bioeconomy, NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829-516 Caparica, PortugalMetal-dependent formate dehydrogenases (Fdh) catalyze the reversible conversion of CO<sub>2</sub> to formate, with unrivalled efficiency and selectivity. However, the key catalytic aspects of these enzymes remain unknown, preventing us from fully benefiting from their capabilities in terms of biotechnological applications. Here, we report a time-resolved characterization by X-ray crystallography of the <i>Desulfovibrio vulgaris</i> Hildenborough SeCys/W-Fdh during formate oxidation. The results allowed us to model five different intermediate structures and to chronologically map the changes occurring during enzyme reduction. Formate molecules were assigned for the first time to populate the catalytic pocket of a Fdh. Finally, the redox reversibility of <i>Dv</i>FdhAB in crystals was confirmed by reduction and reoxidation structural studies.https://www.mdpi.com/1422-0067/24/1/476formate dehydrogenaseCO<sub>2</sub> reductionX-ray crystallographymolybdopterintungsten cofactorredox enzymes |
| spellingShingle | Guilherme Vilela-Alves Rita Rebelo Manuel Ana Rita Oliveira Inês Cardoso Pereira Maria João Romão Cristiano Mota Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme Reoxidation International Journal of Molecular Sciences formate dehydrogenase CO<sub>2</sub> reduction X-ray crystallography molybdopterin tungsten cofactor redox enzymes |
| title | Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme Reoxidation |
| title_full | Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme Reoxidation |
| title_fullStr | Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme Reoxidation |
| title_full_unstemmed | Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme Reoxidation |
| title_short | Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme Reoxidation |
| title_sort | tracking w formate dehydrogenase structural changes during catalysis and enzyme reoxidation |
| topic | formate dehydrogenase CO<sub>2</sub> reduction X-ray crystallography molybdopterin tungsten cofactor redox enzymes |
| url | https://www.mdpi.com/1422-0067/24/1/476 |
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