Structural analysis of wild-type and Val120Thr mutant <i>Candida boidinii</i> formate dehydrogenase by X-ray crystallography
Category
Published on
Type
journal-article
Author
Mehmet Gul and Busra Yuksel and Huri Bulut and Hasan DeMirci
Citation
Gul, M., Yuksel, B., Bulut, H., & DeMirci, H. (2023). Structural analysis of wild-type and Val120Thr mutant Candida boidinii formate dehydrogenase by X-ray crystallography. Acta Crystallographica Section D Structural Biology, 79(11), 1010–1017. https://doi.org/10.1107/s2059798323008070
Abstract
Candida boidinii NAD+-dependent formate dehydrogenase (CbFDH) has gained significant attention for its potential application in the production of biofuels and various industrial chemicals from inorganic carbon dioxide. The present study reports the atomic X-ray crystal structures of wild-type CbFDH at cryogenic and ambient temperatures, as well as that of the Val120Thr mutant at cryogenic temperature, determined at the Turkish Light Source `Turkish DeLight'. The structures reveal new hydrogen bonds between Thr120 and water molecules in the active site of the mutant CbFDH, suggesting increased stability of the active site and more efficient electron transfer during the reaction. Further experimental data is needed to test these hypotheses. Collectively, these findings provide invaluable insights into future protein-engineering efforts that could potentially enhance the efficiency and effectiveness of CbFDH.
DOI
Funding
NSF-STC Biology with X-ray Lasers (NSF-1231306)
