Aspartic acid substitutions affect proton translocation by bacteriorhodopsin.

Ítems similars

• Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation.
  per: Mogi, T, et al.
  Publicat: (1987)
• Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin.
  per: Otto, H, et al.
  Publicat: (1989)
• Replacement of aspartic residues 85, 96, 115, or 212 affects the quantum yield and kinetics of proton release and uptake by bacteriorhodopsin.
  per: Marinetti, T, et al.
  Publicat: (1989)
• 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.
  per: Otto, H, et al.
  Publicat: (1990)
• Role of aspartate-96 in proton translocation by bacteriorhodopsin.
  per: Gerwert, K, et al.
  Publicat: (1989)