Intramolecular charge transfer in the bacteriorhodopsin mutants Asp85-->Asn and Asp212-->Asn: effects of pH and anions.

Podobne zapisy

• 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.
  od: Otto, H, i wsp.
  Wydane: (1990)
• Uv-visible spectroscopy of bacteriorhodopsin mutants: substitution of Arg-82, Asp-85, Tyr-185, and Asp-212 results in abnormal light-dark adaptation.
  od: Duñach, M, i wsp.
  Wydane: (1990)
• Proton transport by a bacteriorhodopsin mutant, aspartic acid-85-->asparagine, initiated in the unprotonated Schiff base state.
  od: Dickopf, S, i wsp.
  Wydane: (1995)
• Gene replacement in Halobacterium halobium and expression of bacteriorhodopsin mutants.
  od: Krebs, M P, i wsp.
  Wydane: (1993)
• 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.
  od: Subramaniam, S, i wsp.
  Wydane: (1990)