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Red-shifting mutation of light-driven sodium-pump rhodopsin

Author

Listed:
  • Keiichi Inoue

    (Nagoya Institute of Technology
    Nagoya Institute of Technology
    The University of Tokyo
    PRESTO, Japan Science and Technology Agency)

  • María Carmen Marín

    (Università di Siena
    Bowling Green State University)

  • Sahoko Tomida

    (Nagoya Institute of Technology)

  • Ryoko Nakamura

    (Nagoya Institute of Technology)

  • Yuta Nakajima

    (Nagoya Institute of Technology)

  • Massimo Olivucci

    (Università di Siena
    Bowling Green State University
    UMR 7504 Université de Strasbourg-CNRS
    Université de Strasbourg)

  • Hideki Kandori

    (Nagoya Institute of Technology
    Nagoya Institute of Technology)

Abstract

Microbial rhodopsins are photoreceptive membrane proteins that transport various ions using light energy. While they are widely used in optogenetics to optically control neuronal activity, rhodopsins that function with longer-wavelength light are highly demanded because of their low phototoxicity and high tissue penetration. Here, we achieve a 40-nm red-shift in the absorption wavelength of a sodium-pump rhodopsin (KR2) by altering dipole moment of residues around the retinal chromophore (KR2 P219T/S254A) without impairing its ion-transport activity. Structural differences in the chromophore of the red-shifted protein from that of the wildtype are observed by Fourier transform infrared spectroscopy. QM/MM models generated with an automated protocol show that the changes in the electrostatic interaction between protein and chromophore induced by the amino-acid replacements, lowered the energy gap between the ground and the first electronically excited state. Based on these insights, a natural sodium pump with red-shifted absorption is identified from Jannaschia seosinensis.

Suggested Citation

  • Keiichi Inoue & María Carmen Marín & Sahoko Tomida & Ryoko Nakamura & Yuta Nakajima & Massimo Olivucci & Hideki Kandori, 2019. "Red-shifting mutation of light-driven sodium-pump rhodopsin," Nature Communications, Nature, vol. 10(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10000-x
    DOI: 10.1038/s41467-019-10000-x
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    Cited by:

    1. Omer Adir & Mia R. Albalak & Ravit Abel & Lucien E. Weiss & Gal Chen & Amit Gruber & Oskar Staufer & Yaniv Kurman & Ido Kaminer & Jeny Shklover & Janna Shainsky-Roitman & Ilia Platzman & Lior Gepstein, 2022. "Synthetic cells with self-activating optogenetic proteins communicate with natural cells," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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