@article {Vilela-Alves:no5205,
	title = {{Structural and biochemical characterization of the M405S variant of {\i}t Desulfovibrio vulgaris} formate dehydrogenase}},
	journal = {Acta Crystallographica Section F},
	volume = {80},
	number = {5},
	year = {2024},
	note = {n/a},
	month = {May},
	pages = {98{\textendash}106},
	abstract = {<p>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 {\i}t Desulfovibrio vulgaris} formate dehydrogenase AB ({\i}t 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.</p>
},
	keywords = {Catalysis, CO2 reduction, Desulfovibrio vulgaris, metal-dependent formate dehydrogenases, Mo/W enzymes, X-ray crystallography},
	doi = {10.1107/S2053230X24003911},
	url = {https://doi.org/10.1107/S2053230X24003911},
	author = {Vilela-Alves, Guilherme and Manuel, Rita Rebelo and Pedrosa, Neide and Cardoso Pereira, In{\^e}s A. and Rom{\~a}o, Maria Jo{\~a}o and Mota, Cristiano}
}
