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.

Antzeko izenburuak

• Uv-visible spectroscopy of bacteriorhodopsin mutants: substitution of Arg-82, Asp-85, Tyr-185, and Asp-212 results in abnormal light-dark adaptation.
  nork: Duñach, M, et al.
  Argitaratua: (1990)
• Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation.
  nork: Subramaniam, S, et al.
  Argitaratua: (1990)
• Locations of Arg-82, Asp-85, and Asp-96 in helix C of bacteriorhodopsin relative to the aqueous boundaries.
  nork: Greenhalgh, D A, et al.
  Argitaratua: (1991)
• Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle.
  nork: Brown, L S, et al.
  Argitaratua: (1993)
• Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin.
  nork: Otto, H, et al.
  Argitaratua: (1989)