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Color Tuning in Retinylidene Proteins

  • Chapter
Optogenetics

Abstract

Retinylidene proteins (also called rhodopsins) are membrane-embedded photoreceptors that contain a vitamin A aldehyde linked to a lysine residue by a Schiff base as their light-sensing chromophore. The chromophore is surrounded by seven-transmembrane α-helices and absorbs light at different wavelengths due to differences in the electronic energy gap between its ground and excited states. The variation in the wavelength of maximal absorption (λmax: 360–620 nm) of rhodopsins arises due to interaction between the apoprotein (opsin) and the retinyl chromophore, the ‘opsin shift’. This chapter reviews the color tuning mechanisms in type-1 microbial and type-2 animal rhodopsins as revealed mainly by our experimental and theoretical studies.

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Authors and Affiliations

  1. Department of Frontier Materials, Nagoya Institute of Technology, Nagoya, 466-8555, Japan

    Kota Katayama

  2. Department of Chemistry, Yale University, New Haven, CT, 06520-8107, USA

    Sivakumar Sekharan

  3. Division of Pharmaceutical Sciences, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, 1-1-1 Tsushima-naka, Kita-ku, Okayama, 700-8530, Japan

    Yuki Sudo PhD

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  1. Kota Katayama
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  2. Sivakumar Sekharan
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  3. Yuki Sudo PhD
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Correspondence to Yuki Sudo PhD .

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Editors and Affiliations

  1. Department of Developmental Biology and Neuroscience, Tohoku University Graduate School of Life Sciences, Sendai, Japan

    Hiromu Yawo

  2. Department of Frontier Materials, Nagoya Institute of Technology, Nagoya, Aichi, Japan

    Hideki Kandori

  3. National Institutes of Natural Sciences, Tokyo, Japan

    Amane Koizumi

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Katayama, K., Sekharan, S., Sudo, Y. (2015). Color Tuning in Retinylidene Proteins. In: Yawo, H., Kandori, H., Koizumi, A. (eds) Optogenetics. Springer, Tokyo. https://doi.org/10.1007/978-4-431-55516-2_7

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