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

Ítems similars

• The role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis; A NMR study()
  per: Peng, Dungeng, et al.
  Publicat: (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
  per: Liu, Yangzhong, et al.
  Publicat: (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
  per: Ma, Li-Hua, et al.
  Publicat: (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
  per: Ma, Li-Hua, et al.
  Publicat: (2006)
• Coupling of the Distal H-bond Network to the Exogenous Ligand in Substrate-bound, Resting State Human Heme Oxygenase
  per: Peng, Dungeng, et al.
  Publicat: (2009)