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Interaction of tyrosine residues with the chromophore in bacteriorhodopsin

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Bioscience Reports

Abstract

We previously reported that the absorption spectrum at low temperatures of iodinated bacteriorhodopsin can be separated into four components with maxima at shorter wavelengths than in native bacteriorhodopsin. In this study, the time course of the formation of each spectral component after iodination was analyzed, revealing that these four components correspond to four different iodinated states of tyrosine residues interacting with the retinal chromophore of bacteriorhodopsin. Therefore at least two tyrosine residues interact with the chromophore of bacteriorhodopsin.

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Authors and Affiliations

  1. Department of Physics, Faculty of Science, Tohoku University, Aobayama, 980, Sendai, Japan

    Kazuo Takeda, Tatsuo Iwasa, Fumio Tokunaga & Lester Packer

  2. Membrane Bioenergetics Group, Applied Sciences Division, Lawrence Berkeley Laboratory, University of California, Berkeley, 94720, Berkeley, California, USA

    Kazuo Takeda, Tatsuo Iwasa, Fumio Tokunaga & Lester Packer

Authors
  1. Kazuo Takeda
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  2. Tatsuo Iwasa
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  3. Fumio Tokunaga
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  4. Lester Packer
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Takeda, K., Iwasa, T., Tokunaga, F. et al. Interaction of tyrosine residues with the chromophore in bacteriorhodopsin. Biosci Rep 5, 615–623 (1985). https://doi.org/10.1007/BF01117075

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  • DOI: https://doi.org/10.1007/BF01117075

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