Proton transport by a bacteriorhodopsin mutant, aspartic acid-85-->asparagine, initiated in the unprotonated Schiff base state.

Ítems similars

• Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin.
  per: Otto, H, et al.
  Publicat: (1989)
• Intramolecular charge transfer in the bacteriorhodopsin mutants Asp85-->Asn and Asp212-->Asn: effects of pH and anions.
  per: Moltke, S, et al.
  Publicat: (1995)
• Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement.
  per: Holz, M, 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)
• Gene replacement in Halobacterium halobium and expression of bacteriorhodopsin mutants.
  per: Krebs, M P, et al.
  Publicat: (1993)