Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network.

@article{Rammelsberg1998BacteriorhodopsinsIP,
  title={Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network.},
  author={Robin Rammelsberg and Gregor Huhn and Mathias L{\"u}bben and Klaus Gerwert},
  journal={Biochemistry},
  year={1998},
  volume={37 14},
  pages={5001-9}
}
In its proton-pumping photocycle, bacteriorhodopsin releases a proton to the extracellular surface at pH 7 in the transition from intermediate L to intermediate M. The proton-release group, named XH, was assigned in low-temperature FT-IR studies to a single residue, E204 [Brown, L. S., Sasaki, J., Kandori, H., Maeda, A., Needleman, R. , and Lanyi, J. K. (1995) J. Biol. Chem. 270, 27122-27126]. The time-resolved room-temperature step-scan FT-IR photocycle studies on wild-type and E204Q-, and… CONTINUE READING

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