Structural and biochemical characterization of the M405S variant of Desulfovibrio vulgaris formate dehydrogenase

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 dehydrogenas...

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Published in:Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2024-05, Vol.80 (5), p.98-106
Main Authors: Vilela-Alves, Guilherme, Rebelo Manuel, Rita, Pedrosa, Neide, Cardoso Pereira, Inês A., Romão, Maria João, Mota, Cristiano
Format: Article
Language:English
Subjects:
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
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Summary: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.
ISSN:2053-230X
2053-230X
DOI:10.1107/S2053230X24003911