N₂H₂ binding to the nitrogenase FeMo cluster studied by QM/MM methods.

ABSTRACT: We have made a systematic combined quantum mechanical and molecular mechanical (QM/MM) investigation of possible structures of the N₂ bound state of nitrogenase. We assume that N₂ is immediately protonated to a N₂H₂ state, thereby avoiding the problem of determining the position of the protons in the cluster. We have systematically studied both end-on and side-on structures, as well as both HNNH and NNH₂ states. Our results indicate that the binding of N₂H₂ is determined more by interactions and steric clashes with the surrounding protein than by the intrinsic preferences of the ligand and the cluster. The best binding mode with both the TPSS and B3LYP density-functional theory methods has trans-HNNH terminally bo

SUBMITTER: Cao L 

PROVIDER: S-EPMC7186253 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature