1. Stereospecificity of hydride transfer and molecular docking in FMN‐dependent NADH‐indigo reductase of Bacillus smithii
- Author
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Haruhiko Sakuraba, Tomohiro Araki, Kazunari Yoneda, and Toshihisa Ohshima
- Subjects
0301 basic medicine ,FMN Reductase ,Stereochemistry ,QH301-705.5 ,Flavin Mononucleotide ,Flavin mononucleotide ,Bacillus ,Reductase ,FMN‐dependent NADH‐indigo reductase ,Indigo Carmine ,Molecular Docking Simulation ,General Biochemistry, Genetics and Molecular Biology ,Indigo ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,Stereospecificity ,Moiety ,Biology (General) ,Research Articles ,Nicotinamide ,Hydride ,NAD ,030104 developmental biology ,chemistry ,030220 oncology & carcinogenesis ,cofactor stereospecificity ,H‐NMR ,Research Article - Abstract
In this study, we investigated the stereospecificity of hydride transfer from NADH to flavin mononucleotide (FMN) in reactions catalyzed by the FMN‐dependent NADH‐indigo reductase expressed by thermophilic Bacillus smithii. We performed 1H‐NMR spectroscopy using deuterium‐labeled NADH (4R‐2H‐NADH) and molecular docking simulations to reveal that the pro‐S hydrogen at the C4 position of the nicotinamide moiety in NADH was specifically transferred to the flavin‐N5 atom of FNM. Altogether, our findings may aid in the improvement of the indigo dyeing (Aizome) process., The stereospecificity of hydride transfer from NADH to flavin mononucleotide (FMN) in reactions catalyzed by the FMN‐dependent NADH‐indigo reductase from the thermophilic bacterium Bacillus smithii was studied. Both analyses of 1H‐NMR spectroscopy using deuterium‐labeled NADH (4R‐2H‐NADH) and molecular docking simulations showed that the pro‐S hydrogen of NADH was specifically transferred to the flavin‐N5 atom of FNM.
- Published
- 2021