Structural analysis of wild-type and Val120Thr mutant Candida boidinii formate dehydrogenase by X-ray crystallography

  • 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. The present study reports the atomic X-ray crystal structures of the wild-type CbFDH at cryogenic and ambient temperatures as well as 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 mutant CbFDH's active site, 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, our findings provide invaluable insights into future protein engineering efforts that could potentially enhance the efficiency and effectiveness of CbFDH.

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Metadaten
Author:Mehmet GulORCiD, Büşra YükselORCiD, Huri BulutORCiD, Hasan DeMirciORCiD
URN:urn:nbn:de:hebis:30:3-756372
URL:https://www.biorxiv.org/content/10.1101/2022.12.25.521900v2
DOI:https://doi.org/10.1101/2022.12.25.521900
Parent Title (English):bioRxiv
Document Type:Preprint
Language:English
Year of Completion:2023
Year of first Publication:2023
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2023/09/12
Issue:2022.12.25.521900 Version 2
Edition:Version 2
Page Number:23
HeBIS-PPN:512115265
Institutes:Biochemie, Chemie und Pharmazie
Angeschlossene und kooperierende Institutionen / MPI für Biophysik
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Licence (German):License LogoCreative Commons - CC BY-NC - Namensnennung - Nicht kommerziell 4.0 International