Engineering the biomimetic cofactors of NMNH for cytochrome P450 BM3 based on binding conformation refinement.

ABSTRACT: Cytochrome P450 BM3 (BM3) is an important oxidoreductase that is widely used in drug synthesis, chemical synthesis, and other industries. However, as BM3 unquestionably increases costs by consuming a natural cofactor that unstably provides electrons, an alternative biomimetic cofactor with simpler structures represented by nicotinamide mononucleotide (NMNH) has been utilized. Currently, few reports exist on artificially modified BM3 enzymes using NMNH, especially regarding theoretical simulation and calculation. With the cognition of the mechanism in mind, we propose a strategy that optimizes and refines catalytic conformation. Based on constrained molecular dynamics simulation, the distance between N-5 of FAD flavin and C-4 of NMNH is used as a cue for the determination of improved confor

SUBMITTER: Liu Y 

PROVIDER: S-EPMC8696588 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature