Open AccessStereospecificity of hydride transfer and molecular docking in FMN‐dependent NADH‐indigo reductase of Bacillus smithii
Author(s) -
Yoneda Kazunari,
Sakuraba Haruhiko,
Araki Tomohiro,
Ohshima Toshihisa
Publication year - 2021
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.13200
Subject(s) - flavin mononucleotide , chemistry , stereospecificity , stereochemistry , flavin group , moiety , active site , reductase , porphyrin , docking (animal) , nad+ kinase , biochemistry , enzyme , catalysis , medicine , nursing
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 1 H‐NMR spectroscopy using deuterium‐labeled NADH (4 R ‐ 2 H‐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.