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How Catalizes Azide Proton-Pumping in D96N Mutated Bacteriorhodopsin?

  • J. le Coutre
  • K. Gerwert
Conference paper
Part of the Springer Proceedings in Physics book series (SPPHY, volume 74)

Abstract

Bacteriorhodopsin (bR) from halobacterium salinarium converts light energy into chemical energy by pumping protons across the cytoplasmic membrane and thereby creating a proton gradient. The chromophor, all-trans-retinal, is covalently linked to one of the seven transmembrane helices via a protonated Schiff-base. After lightexcitation the chromophore isomerizes and the protein undergoes a photocycle during which one proton is transferred to the extracellular side. Using timeresolved FTIR-techniques two aspartic residues have been identified to be crucial for proton-pumping [1]. D85 works as internal proton-acceptor receiving a proton from the Schiffbase and D96 works as internal proton-donor to the Schiflbase.

Keywords

Chemical Energy Light Energy Cytoplasmic Membrane Transmembrane Helix Proton Gradient 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

  1. [1]
    Gerwert K. (1992), Biochimica et Biophysica Acta 1101: 147–153Google Scholar
  2. [2]
    Tittor J., Soell C., Oesterhelt D., Butt H.-J. and Bamberg E. (1989), The Journal 8: 3477–3482Google Scholar
  3. [3]
    le Coutre J. and Gerwert K. (1992), Proceedings of the Vih Internatio al Conference on Retinal Proteins (J.L. Rigaud ed.): 127–130Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1994

Authors and Affiliations

  • J. le Coutre
    • 1
  • K. Gerwert
    • 1
  1. 1.Max-Planck-Institut für molekulare PhysiologieDortmundGermany

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