Perturbed interaction between residues 85 and 204 in Tyr-185-->Phe and Asp-85-->Glu bacteriorhodopsins
- 1 December 1996
- journal article
- research article
- Published by Elsevier in Biophysical Journal
- Vol. 71 (6) , 3392-3398
- https://doi.org/10.1016/s0006-3495(96)79532-2
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- A Linkage of the pKa's of asp-85 and glu-204 Forms Part of the Reprotonation Switch of BacteriorhodopsinBiochemistry, 1996
- Glutamic Acid 204 is the Terminal Proton Release Group at the Extracellular Surface of BacteriorhodopsinPublished by Elsevier ,1995
- The two pKa's of aspartate-85 and control of thermal isomerization and proton release in the arginine-82 to lysine mutant of bacteriorhodopsin.1995
- Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycleBiophysical Journal, 1993
- FTIR difference spectroscopy of the bacteriorhodopsin mutant Tyr-185 .fwdarw. Phe: Detection of a stable O-like species and characterization of its photocycle at low temperatureBiochemistry, 1993
- Static and time-resolved absorption spectroscopy of the bacteriorhodopsin mutant Tyr-185 .fwdarw. Phe: Evidence for an equilibrium between bR570 and an O-like speciesBiochemistry, 1993
- The retinylidene Schiff base counterion in bacteriorhodopsin.Journal of Biological Chemistry, 1991
- Redshift of the purple membrane absorption band and the deprotonation of tyrosine residues at high pHBiophysical Journal, 1991
- 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.Proceedings of the National Academy of Sciences, 1990
- Effect of acid pH on the absorption spectra and photoreactions of bacteriorhodopsinBiochemistry, 1979