Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation.

Similar Items

• Aspartic acid substitutions affect proton translocation by bacteriorhodopsin.
  od: Mogi, T, i dr.
  Izdano: (1988)
• Effect of genetic modification of tyrosine-185 on the proton pump and the blue-to-purple transition in bacteriorhodopsin.
  od: Jang, D J, i dr.
  Izdano: (1990)
• Mechanism of light-dependent proton translocation by bacteriorhodopsin.
  od: Krebs, M P, i dr.
  Izdano: (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 dr.
  Izdano: (1990)
• 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 dr.
  Izdano: (1990)