Cation binding sites on the projected structure of bacteriorhodopsin.

@article{Katre1986CationBS,
  title={Cation binding sites on the projected structure of bacteriorhodopsin.},
  author={Nandini V. Katre and Yoshikazu Kimura and Robert M Stroud},
  journal={Biophysical journal},
  year={1986},
  volume={50 2},
  pages={
          277-84
        }
}
Divalent cations are involved in the function of bacteriorhodopsin (bR) as a light-driven proton pump. If cations are removed from purple membranes they become blue. Divalent cations such as Ca2+ or Pb2+ or trivalent ions, can be stoichiometrically titrated back on to these deionized membranes. The color transitions as a function of ion concentration for Ca2+ or Pb2+ are precisely comparable and indicate that approximately three stoichiometric equivalents of cations are required to effect the… CONTINUE READING

References

Publications referenced by this paper.
SHOWING 1-10 OF 12 REFERENCES

Attachment site of retinal in bacteriorhodopsin

  • Stroud.
  • Proc. Natl. Acad. Sci. USA. 78:4068-4072. Kimura, Y., A.
  • 1981
VIEW 5 EXCERPTS
HIGHLY INFLUENTIAL

Path of the polypeptide in bacteriorhodopsin.

VIEW 1 EXCERPT
HIGHLY INFLUENTIAL

Cation binding by bacteriorhodopsin.

Importance of bound divalent cations to the tyrosine deprotonation during the photocycle of bacteriorhodopsin.

Location of cation binding sites in the tertiary structure of purple membranes from halobacteria

  • Mol. Biol
  • 1984

Quantitative analysis of nucleic acids, proteins and viruses by Raman band deconvolution

  • Agard.
  • Biophys. J. 46:763-768. Tsuji, K., and K. Rosenheck. 1979. The low pH
  • 1984

Bacteriorhodopsin and related pigments of halobacteria.

VIEW 1 EXCERPT

Location of the carboxyl terminus of bacteriorhodopsin in purple membrane

  • Henderson.
  • Biophys. J. 39:233-239.
  • 1982
VIEW 2 EXCERPTS

Site of attachment of retinal in bacteriorhodopsin.

VIEW 1 EXCERPT