Decoupling of photo- and proton cycle in the Asp85-->Glu mutant of bacteriorhodopsin.

Podobne zapisy

• 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)
• Inversion of proton translocation in bacteriorhodopsin mutants D85N, D85T, and D85,96N.
  od: Tittor, J, i wsp.
  Wydane: (1994)
• Perturbed interaction between residues 85 and 204 in Tyr-185-->Phe and Asp-85-->Glu bacteriorhodopsins.
  od: Richter, H T, i wsp.
  Wydane: (1996)
• Roles of cytoplasmic arginine and threonine in chloride transport by the bacteriorhodopsin mutant D85T.
  od: Paula, S, i wsp.
  Wydane: (2001)
• Two groups control light-induced schiff base deprotonation and the proton affinity of asp(85) in the Arg(82)His mutant of bacteriorhodopsin
  od: Imasheva, ES, i wsp.
  Wydane: (1999)