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Zinc Binding to Heliorhodopsin.

Masanori Hashimoto1, Kota Katayama1,2, Yuji Furutani1,2

  • 1Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.

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Heliorhodopsins (HeRs) are new light sensors. This study shows zinc ions (Zn2+) bind to HeR, causing structural changes and suggesting a role in modifying HeR function.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Heliorhodopsins (HeRs) represent a novel rhodopsin family with an inverted membrane topology.
  • Unlike other rhodopsins, HeRs lack ion-transport activity, and their function as light sensors is not fully understood.
  • Previous studies indicated HeRs do not bind monovalent cations or anions.

Purpose of the Study:

  • To investigate potential ion binding and functional modifications of Heliorhodopsins.
  • To explore the interaction of divalent cations with HeR, specifically focusing on Zn2+.

Main Methods:

  • Attenuated Total Reflectance Fourier Transform Infrared (ATR-FTIR) spectroscopy was employed to analyze HeR structure and ion binding.
  • Spectroscopic analysis was performed on HeR from *Thermoplasmatales archaeon* (TaHeR) and HeR 48C12.

Main Results:

  • ATR-FTIR spectroscopy revealed specific binding of Zn2+ to TaHeR with a dissociation constant (Kd) of 0.2 mM.
  • Zn2+ binding induced helical structural perturbations in HeR without altering its spectral color.
  • While other divalent cations showed ion-specific FTIR spectra, only Zn2+ caused these specific helical changes.

Conclusions:

  • Zinc ions (Zn2+) bind to Heliorhodopsins, indicating a potential role for this cation in HeR function.
  • The observed structural perturbations suggest that Zn2+ may modify the light-sensing capabilities or other functions of HeR.
  • These findings open new avenues for understanding the biological roles of Heliorhodopsins and their interactions with metal ions.