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.

Eitemau Tebyg

• 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.
  gan: Otto, H, et al.
  Cyhoeddwyd: (1990)
• Locations of Arg-82, Asp-85, and Asp-96 in helix C of bacteriorhodopsin relative to the aqueous boundaries.
  gan: Greenhalgh, D A, et al.
  Cyhoeddwyd: (1991)
• Uv-visible spectroscopy of bacteriorhodopsin mutants: substitution of Arg-82, Asp-85, Tyr-185, and Asp-212 results in abnormal light-dark adaptation.
  gan: Duñach, M, et al.
  Cyhoeddwyd: (1990)
• Decoupling of photo- and proton cycle in the Asp85-->Glu mutant of bacteriorhodopsin.
  gan: Heberle, J, et al.
  Cyhoeddwyd: (1993)
• Two groups control light-induced schiff base deprotonation and the proton affinity of asp(85) in the Arg(82)His mutant of bacteriorhodopsin
  gan: Imasheva, ES, et al.
  Cyhoeddwyd: (1999)