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}
}
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… Expand
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TLDR
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TLDR
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