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

Journal Article · · Acta Crystallographica. Section D. Structural Biology
 [1];  [2];  [3];  [4]
  1. Koc Univ., Istanbul (Turkey); SLAC
  2. Koc Univ., Istanbul (Turkey); Max Planck Institute of Biophysics, Frankfurt (Germany)
  3. Istinye Univ., Istanbul (Turkey)
  4. Koc Univ., Istanbul (Turkey); SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States). Photon Ultrafast Laser Science and Engineering Institute (PULSE)

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.

Research Organization:
SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC); National Science Foundation (NSF)
Grant/Contract Number:
AC02-76SF00515
OSTI ID:
2327111
Journal Information:
Acta Crystallographica. Section D. Structural Biology, Journal Name: Acta Crystallographica. Section D. Structural Biology Journal Issue: 11 Vol. 79; ISSN 2059-7983
Publisher:
International Union of CrystallographyCopyright Statement
Country of Publication:
United States
Language:
English

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