TY - JOUR
T1 - Structural and biochemical characterization of the M405S variant of Desulfovibrio vulgaris formate dehydrogenase
AU - Vilela-Alves, Guilherme
AU - Manuel, Rita Rebelo
AU - Pedrosa, Neide
AU - Pereira, Inês A. Cardoso
AU - Romão, Maria João
AU - Mota, Cristiano
N1 - Publisher Copyright:
© 2024 International Union of Crystallography. All rights reserved.
This work is financed by national funds from Fundação para a Ciência e a Tecnologia, I.P. (FCT) through fellowship 2023.00286.BD (to V-AG), project PTDC/BII-BBF/2050/2020,
the Research Unit on Applied Molecular Biosciences (UCIBIO; UIDP/04378/2020 and UIDB/04378/2020) and MOSTMICRO-ITQB (UIDB/04612/2020 and UIDP/04612/
2020) and Associate Laboratories Institute for Health and Bioeconomy i4HB (LA/P/0140/2020) and LS4FUTURE (LA/P/0087/2020).
PY - 2024/5
Y1 - 2024/5
N2 - 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.
AB - 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.
KW - catalysis
KW - CO reduction
KW - Desulfovibrio vulgaris
KW - metal-dependent formate dehydrogenases
KW - Mo/W enzymes
KW - X-ray crystallography
UR - http://www.scopus.com/inward/record.url?scp=85194979131&partnerID=8YFLogxK
U2 - 10.1107/S2053230X24003911
DO - 10.1107/S2053230X24003911
M3 - Article
C2 - 38699971
AN - SCOPUS:85194979131
SN - 2053-230X
VL - 80
SP - 98
EP - 106
JO - Acta Crystallographica Section F: Structural Biology Communications
JF - Acta Crystallographica Section F: Structural Biology Communications
IS - Pt 5
ER -