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Specific zinc binding to heliorhodopsin.

Masanori Hashimoto1, Koichi Miyagawa2, Manish Singh1

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Zinc ions (Zn2+) bind to heliorhodopsins (HeRs) from Thermoplasmatales archaeon (TaHeR), altering its thermal stability and photocycle. This binding, primarily involving glutamate 150 (E150), occurs on the cytoplasmic side and may modify HeR

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Proteins

Background:

  • Heliorhodopsins (HeRs) possess an inverted membrane topology compared to other rhodopsins.
  • Their slow photocycle suggests a light-sensing role, but their exact function remains elusive.
  • Previous studies indicated Zn2+ binding to HeRs, causing helical structural changes.

Purpose of the Study:

  • To investigate the effect of Zn2+ binding on the structure and function of TaHeR.
  • To identify the specific binding site of Zn2+ in TaHeR.
  • To elucidate the functional implications of Zn2+ interaction with TaHeR.

Main Methods:

  • Attenuated Total Reflectance-Fourier Transform Infrared (ATR-FTIR) spectroscopy to monitor structural changes.
  • Site-directed mutagenesis to probe the Zn2+ binding site.
  • Molecular Dynamics (MD) simulations to model Zn2+ coordination.

Main Results:

  • Zn2+ binding decreases TaHeR thermal stability and slows M-cycle decay (back proton transfer).
  • ATR-FTIR and mutagenesis identified Glutamate 150 (E150) as crucial for Zn2+ binding.
  • MD simulations revealed a cytoplasmic Zn2+ binding site involving E150 and water molecules.

Conclusions:

  • Zn2+ specifically binds to TaHeR at the cytoplasmic side, involving E150.
  • Zn2+ binding impacts TaHeR's structural integrity and dynamics.
  • This interaction may modulate the yet-unknown function of heliorhodopsins.