The role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis; A NMR study()

Παρόμοια τεκμήρια

• 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
  ανά: Peng, Dungeng, κ.ά.
  Έκδοση: (2011)
• 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
  ανά: Liu, Yangzhong, κ.ά.
  Έκδοση: (2006)
• 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
  ανά: Ma, Li-Hua, κ.ά.
  Έκδοση: (2006)
• (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
  ανά: Ma, Li-Hua, κ.ά.
  Έκδοση: (2006)
• (1)H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure
  ανά: Ma, Li-Hua, κ.ά.
  Έκδοση: (2008)