Modulation of the axial water hydrogen-bonding properties by chemical modification of the substrate in resting state, substrate-bound heme oxygenase from Neisseria meningitidis; Coupling to the distal H-bond network via ordered water molecules

Lignende værker

• (1)H NMR study of the magnetic properties and electronic structure of the hydroxide complex of substrate-bound heme oxygenase from Neisseria meningitidis; Influence of the axial water deprotonation on the distal H-bond network
  af: Ma, Li-Hua, et al.
  Udgivet: (2006)
• The role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis; A NMR study()
  af: Peng, Dungeng, et al.
  Udgivet: (2012)
• Characterization of the spontaneous “aging” of the heme oxygenase from the pathological bacterium Neisseria meningitidis via cleavage of the C-terminus in contact with the substrate; Implications for functional studies and the crystal structure
  af: Liu, Yangzhong, et al.
  Udgivet: (2006)
• Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A (1)H NMR study
  af: Peng, Dungeng, et al.
  Udgivet: (2011)
• Spectroscopic insights into axial ligation and active-site H-bonding in substrate-bound human heme oxygenase-2
  af: Gardner, Jessica D., et al.
  Udgivet: (2010)