Protein changes associated with reprotonation of the Schiff base in the photocycle of Asp96-->Asn bacteriorhodopsin. The MN intermediate with unprotonated Schiff base but N-like protein structure.

@article{Sasaki1992ProteinCA,
  title={Protein changes associated with reprotonation of the Schiff base in the photocycle of Asp96-->Asn bacteriorhodopsin. The MN intermediate with unprotonated Schiff base but N-like protein structure.},
  author={Jun Sasaki and Yoshinori Shichida and Janos K. Lanyi and Akio Maeda},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 29},
  pages={20782-6}
}
The difference Fourier transform infrared spectrum for the N intermediate in the photoreaction of the light-adapted form of bacteriorhodopsin can be recorded at pH 10 at 274 K (Pfefferlé, J.-M., Maeda, A., Sasaki, J., and Yoshizawa, T. (1991) Biochemistry 30, 6548-6556). Under these conditions, Asp96-->Asn bacteriorhodopsin gives a photoproduct which shows changes in protein structure similar to those observed in N of wild-type bacteriorhodopsin. However, decreased intensity of the chromophore… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 12 extracted citations

Atomic resolution structures and the mechanism of ion pumping in bacteriorhodopsin.

Frontiers in bioscience : a journal and virtual library • 2004
View 1 Excerpt

Similar Papers

Loading similar papers…