Structural Analysis of Wild-type and Val120Thr MutantCandida boidiniiFormate Dehydrogenase by X-ray Crystallography

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 A 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.