Acta crystallographica. Section F, Structural biology communications, 2024-05, Vol.80 (5), p.98-106
2024
Volltextzugriff (PDF)
Details
- Autor(en) / Beteiligte
- Titel
- Structural and biochemical characterization of the M405S variant of Desulfovibrio vulgaris formate dehydrogenase
- Ist Teil von
- Acta crystallographica. Section F, Structural biology communications, 2024-05, Vol.80 (5), p.98-106
- Ort / Verlag
- 5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography
- Erscheinungsjahr
- 2024
- Quelle
- Wiley Online Library Journals Frontfile Complete
- Beschreibungen/Notizen
- Molybdenum‐ or tungsten‐dependent formate dehydrogenases have emerged as significant catalysts for the chemical reduction of CO2 to formate, with biotechnological applications envisaged in climate‐change mitigation. The role of Met405 in the active site of Desulfovibrio vulgaris formate dehydrogenase AB (DvFdhAB) has remained elusive. However, its proximity to the metal site and the conformational change that it undergoes between the resting and active forms suggests a functional role. In this work, the M405S variant was engineered, which allowed the active‐site geometry in the absence of methionine Sδ interactions with the metal site to be revealed and the role of Met405 in catalysis to be probed. This variant displayed reduced activity in both formate oxidation and CO2 reduction, together with an increased sensitivity to oxygen inactivation. A crystallographic and biochemical study of the M405S variant of D. vulgaris formate dehydrogenase AB is reported in order to clarify the role of Met405 in catalysis in an enzyme that has applications in climate‐change mitigation tools.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 2053-230XeISSN: 2053-230XDOI: 10.1107/S2053230X24003911Titel-ID: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_11134731
- Format
- –
- Schlagworte
- Bacterial Proteins - chemistry, Bacterial Proteins - genetics, Bacterial Proteins - metabolism, Biotechnology, Carbon dioxide, Carbon Dioxide - chemistry, Carbon Dioxide - metabolism, Catalysis, Catalysts, Catalytic Domain, Chemical reduction, CO2 reduction, Crystallography, X-Ray, Dehydrogenase, Desulfovibrio vulgaris, Desulfovibrio vulgaris - enzymology, Desulfovibrio vulgaris - genetics, Formate dehydrogenase, Formate Dehydrogenases - chemistry, Formate Dehydrogenases - genetics, Formate Dehydrogenases - metabolism, Formates - chemistry, Formates - metabolism, Inactivation, metal‐dependent formate dehydrogenases, Methionine, Mo/W enzymes, Models, Molecular, Molybdenum, Oxidation, Oxidation-Reduction, Research Communications, Structural analysis, Tungsten, X‐ray crystallography