Mutants of Cytochrome P450 Reductase Lacking Either Gly-141 or Gly-143 Destabilize Its FMN Semiquinone

Lignende værker

• Kinetic and Structural Characterization of the Interaction between the FMN Binding Domain of Cytochrome P450 Reductase and Cytochrome c
  af: Huang, Rui, et al.
  Udgivet: (2015)
• Structural and kinetic studies of Asp632 mutants and fully-reduced NADPH-cytochrome P450 oxidoreductase define the role of Asp632 loop dynamics in control of NADPH binding and hydride transfer
  af: Xia, Chuanwu, et al.
  Udgivet: (2018)
• Short-lived neutral FMN and FAD semiquinones are transient intermediates in cryo-reduced yeast NADPH-cytochrome P450 reductase
  af: Davydov, Roman M., et al.
  Udgivet: (2019)
• Structure of cytochrome P450 2B4 with an acetate ligand and an active site hydrogen bond network similar to oxyferrous P450cam
  af: Yang, Yuting, et al.
  Udgivet: (2018)
• Structural and Functional Characterization of a Cytochrome P450 2B4 F429H Mutant with an Axial Thiolate–Histidine Hydrogen Bond
  af: Yang, Yuting, et al.
  Udgivet: (2014)