{Structural and biochemical characterization of the M405S variant of ıt Desulfovibrio vulgaris} formate dehydrogenase}
- Citation:
- Vilela-Alves, G, Manuel RR, Pedrosa N, Cardoso Pereira IA, Romão MJ, Mota C. 2024. {Structural and biochemical characterization of the M405S variant of ıt Desulfovibrio vulgaris} formate dehydrogenase}, May. Acta Crystallographica Section F. 80:98–106., Number 5
Abstract:
Molybdenum- or tungsten-dependent formate dehydrogenases have emerged as significant catalysts for the chemical reduction of CO${\sb 2}$ to formate, with biotechnological applications envisaged in climate-change mitigation. The role of Met405 in the active site of ıt Desulfovibrio vulgaris} formate dehydrogenase AB (ıt Dv}FdhAB) 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 S${\sp {$δ$}}$ 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 CO${\sb 2}$ reduction, together with an increased sensitivity to oxygen inactivation.
Notes:
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