In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy.

@article{Zscherp1999InSD,
  title={In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy.},
  author={Christian Zscherp and Ramona Schlesinger and Joerg Tittor and Dieter Oesterhelt and Joachim Heberle},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 10},
  pages={5498-503}
}
Active proton transfer through membrane proteins is accomplished by shifts in the acidity of internal amino acids, prosthetic groups, and water molecules. The recently introduced step-scan attenuated total reflection Fourier-transform infrared (ATR/FT-IR) spectroscopy was employed to determine transient pKa changes of single amino acid side chains of the proton pump bacteriorhodopsin. The high pKa of D96 (>12 in the ground state) drops to 7.1 +/- 0.2 (in 1 M KCl) during the lifetime of the N… CONTINUE READING
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Zscherp et al

  • K. Fahmy, O. Weidlich, +4 authors 5862–5869. Biophysics
  • Proc. Natl. Acad. Sci. USA 96
  • 1999
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