Low temperature FTIR study of the Schiff base reprotonation during the M-to-bR backphotoreaction: Asp 85 reprotonates two distinct types of Schiff base species at different temperatures

Παρόμοια τεκμήρια

• Connectivity of the retinal Schiff base to Asp85 and Asp96 during the bacteriorhodopsin photocycle: the local-access model.
  ανά: Brown, L S, κ.ά.
  Έκδοση: (1998)
• Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle.
  ανά: Brown, L S, κ.ά.
  Έκδοση: (1993)
• Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin.
  ανά: Otto, H, κ.ά.
  Έκδοση: (1989)
• Effects of tryptophan mutation on the deprotonation and reprotonation kinetics of the Schiff base during the photocycle of bacteriorhodopsin.
  ανά: Wu, S, κ.ά.
  Έκδοση: (1992)
• 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.
  ανά: Otto, H, κ.ά.
  Έκδοση: (1990)