Version 1
: Received: 25 December 2022 / Approved: 30 December 2022 / Online: 30 December 2022 (08:03:07 CET)
How to cite:
Gul, M.; Yuksel, B.; Bulut, H.; DeMirci, H. Structural and Dynamic Characterization of Candida boidinii Formate Dehydrogenase by High-Resolution X-ray Crystallography. Preprints2022, 2022120572. https://doi.org/10.20944/preprints202212.0572.v1
Gul, M.; Yuksel, B.; Bulut, H.; DeMirci, H. Structural and Dynamic Characterization of Candida boidinii Formate Dehydrogenase by High-Resolution X-ray Crystallography. Preprints 2022, 2022120572. https://doi.org/10.20944/preprints202212.0572.v1
Gul, M.; Yuksel, B.; Bulut, H.; DeMirci, H. Structural and Dynamic Characterization of Candida boidinii Formate Dehydrogenase by High-Resolution X-ray Crystallography. Preprints2022, 2022120572. https://doi.org/10.20944/preprints202212.0572.v1
APA Style
Gul, M., Yuksel, B., Bulut, H., & DeMirci, H. (2022). Structural and Dynamic Characterization of Candida boidinii Formate Dehydrogenase by High-Resolution X-ray Crystallography. Preprints. https://doi.org/10.20944/preprints202212.0572.v1
Chicago/Turabian Style
Gul, M., Huri Bulut and Hasan DeMirci. 2022 "Structural and Dynamic Characterization of Candida boidinii Formate Dehydrogenase by High-Resolution X-ray Crystallography" Preprints. https://doi.org/10.20944/preprints202212.0572.v1
Abstract
Candida boidinii NAD+-dependent formate dehydrogenase (CbFDH) has gained significant attention for its potential applications in the production of biofuels and various industrial chemicals from inorganic carbon dioxide. In this study, we present an atomic X-ray crystal structure of the apo CbFDH to 1.4 Å resolution determined at cryogenic temperature at the Turkish Light Source, “Turkish DeLight”. This structure offers a comprehensive view of the apo enzyme's dynamics, filling the gaps in our understanding from previous studies. Also, comparison of our high-resolution apo and previously available holo enzyme structures reveals major conformational changes of this dynamic enzyme in the absence and presence of the coenzyme and substrate/inhibitor complexes. Collectively all these information may provide invaluable insights into future protein engineering efforts that could enhance enzymatic activity and stability, potentially increasing its efficiency and effectiveness of CbFDH in industrial processes.
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
