Two groups control light-induced schiff base deprotonation and the proton affinity of asp(85) in the Arg(82)His mutant of bacteriorhodopsin

Gelijkaardige items

• Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle.
  door: Brown, L S, et al.
  Gepubliceerd in: (1993)
• 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)
• Arginine-82 regulates the pKa of the group responsible for the light-driven proton release in bacteriorhodopsin.
  door: Govindjee, R, et al.
  Gepubliceerd in: (1996)
• Titration of aspartate-85 in bacteriorhodopsin: what it says about chromophore isomerization and proton release.
  door: Balashov, S P, et al.
  Gepubliceerd in: (1996)