A suicide mutation affecting proton transfers to high-valent hemes causes inactivation of MauG during catalysis

Lignende værker

• Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-Fe(IV) state of MauG
  af: Ma, Zhongxin, et al.
  Udgivet: (2015)
• Oxidative damage in MauG: implications for control of high-valent iron species and radical propagation pathways
  af: Yukl, Erik T., et al.
  Udgivet: (2013)
• Ascorbate Protects the Di-Heme Enzyme, MauG, Against Self-Inflicted Oxidative Damage by an Unusual Antioxidant Mechanism
  af: Ma, Zhongxin, et al.
  Udgivet: (2017)
• MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis
  af: Shin, Sooim, et al.
  Udgivet: (2013)
• Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away
  af: Feng, Manliang, et al.
  Udgivet: (2017)