Molecular mechanism of vectorial proton translocation by bacteriorhodopsin

@article{Subramaniam2000MolecularMO,
  title={Molecular mechanism of vectorial proton translocation by bacteriorhodopsin},
  author={S. Subramaniam and R. Henderson},
  journal={Nature},
  year={2000},
  volume={406},
  pages={653-657}
}
  • S. Subramaniam, R. Henderson
  • Published 2000
  • Medicine, Chemistry
  • Nature
  • Bacteriorhodopsin, a membrane protein with a relative molecular mass of 27,000, is a light driven pump which transports protons across the cell membrane of the halophilic organism Halobacterium salinarum. The chromophore retinal is covalently attached to the protein via a protonated Schiff base. Upon illumination, retinal is isomerized. The Schiff base then releases a proton to the extracellular medium, and is subsequently reprotonated from the cytoplasm. An atomic model for bacteriorhodopsin… CONTINUE READING
    A three-dimensional movie of structural changes in bacteriorhodopsin
    • 173
    • PDF
    X-ray diffraction of bacteriorhodopsin photocycle intermediates (Review)
    • 65
    Structural dynamics of light-driven proton pumps.
    • 96
    • Highly Influenced
    Deprotonation of D96 in bacteriorhodopsin opens the proton uptake pathway.
    • 28
    • PDF
    Mechanism of primary proton transfer in bacteriorhodopsin.
    • 86
    • Highly Influenced
    • PDF

    References

    Publications referenced by this paper.
    SHOWING 1-10 OF 33 REFERENCES
    Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin
    • 274
    • Highly Influential
    Halorhodopsin is a light-driven chloride pump.
    • 435