Time-Resolved Resonance Raman and Optical Transient Studies on the Photocycle of the Bacteriorhodopsin Mutant ASP 96→ASN

  • W. Eisfeld
  • M. Stockburger
Chapter

Abstract

Bacteriorhodopsin is a retinal-binding protein in the cell membrane of Halobacteria where it acts as a light-driven proton pump. Upon absorption of light, the retinylidene Schiff base chromophore BR570 runs through a series of intermediate states (K, L, M, N, O) and is reconstituted within ~8ms (pH 7, 20°C). This cyclic reaction (“photocycle”) is accompanied by the release of a proton to the extracellular side and the uptake of a proton from the cytoplasmic side. The transfer of the Schiff base proton to the counterion (carboxylate side chain of residue Asp85), i.e. the formation of M, and the reprotonation of the Schiff base (decay of M) are believed to play a key role in proton pumping.

Keywords

Schiff Base Cytoplasmic Side Laser Flash Photolysis Extracellular Side Carboxylate Side Chain 
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.
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References

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Copyright information

© Springer Science+Business Media Dordrecht 1993

Authors and Affiliations

  • W. Eisfeld
    • 1
  • M. Stockburger
    • 1
  1. 1.Max-Planck-Institut für biophysikalische ChemieGöttingenGermany

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