Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle.

Gelijkaardige items

• Connectivity of the retinal Schiff base to Asp85 and Asp96 during the bacteriorhodopsin photocycle: the local-access model.
  door: Brown, L S, et al.
  Gepubliceerd in: (1998)
• Locations of Arg-82, Asp-85, and Asp-96 in helix C of bacteriorhodopsin relative to the aqueous boundaries.
  door: Greenhalgh, D A, et al.
  Gepubliceerd in: (1991)
• Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base.
  door: Otto, H, et al.
  Gepubliceerd in: (1990)
• Two groups control light-induced schiff base deprotonation and the proton affinity of asp(85) in the Arg(82)His mutant of bacteriorhodopsin
  door: Imasheva, ES, et al.
  Gepubliceerd in: (1999)
• Relationship of proton release at the extracellular surface to deprotonation of the schiff base in the bacteriorhodopsin photocycle.
  door: Cao, Y, et al.
  Gepubliceerd in: (1995)