Activity of Bacteriorhodopsin in the Presence of a Large pH Gradient

  • T. Kouyama
  • A. N. Kouyama
  • A. Ikegami
Conference paper
Part of the Springer Proceedings in Physics book series (SPPHY, volume 20)


Bacteriorhodopsin (bR) is a membrane protein found in Halobacterium halobium. Due to the retinal chromophore bound to the apoprotein via a protonated Schiff base linkage, bR shows a strong absorption band in the visible region. Light excitation of the chromophore initiates a photochemical cycle of bR, through which protons are actively translocated from the cytoplasmic side to the outside, thereby generating a pH gradient across the plasma membrane [1]. It has been shown that formation of a yellow intermediate M412 is accompanied with deprotonation of the Schiff base [2], and it has been widely accepted that its deprotonation (and subsequent reprotonation) is coupled with a unidirectional flow of protons in bR.


Proton Release Proton Pump Activity Vesicle Interior Photochemical Cycle Envelope Vesicle 
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Copyright information

© Springer-Verlag Berlin Heidelberg 1987

Authors and Affiliations

  • T. Kouyama
    • 1
  • A. N. Kouyama
    • 1
  • A. Ikegami
    • 1
  1. 1.The Institute of Physical and Chemical ResarchWako-shi, SaitamaJapan

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