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Masayo Iwaki, Kohei Takeshita, Hiroko X Kondo1,2

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Summary

Zinc ions (Zn2+) inhibit the voltage-gated proton channel (Hv1/VSOP) by binding to its extracellular region. Attenuated total reflection-Fourier transform infrared (ATR-FTIR) spectroscopy revealed Zn2+ coordination with histidine and carboxylate groups, forming a tetrahedral structure.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • The voltage-gated proton channel, Hv1/VSOP, plays a crucial role in cellular pH homeostasis and signaling.
  • Hv1/VSOP activity is modulated by extracellular factors, including zinc ions (Zn2+).
  • Understanding the precise Zn2+ binding mechanism is essential for elucidating Hv1/VSOP function and developing targeted therapeutics.

Purpose of the Study:

  • To investigate the coordination structure of Zn2+ binding to the extracellular region of Hv1/VSOP.
  • To elucidate the specific amino acid residues and coordination geometry involved in Zn2+ inhibition.

Main Methods:

  • Attenuated total reflection-Fourier transform infrared (ATR-FTIR) spectroscopy was employed to monitor protein structural changes upon Zn2+ binding.
  • Difference spectra were analyzed to identify specific vibrational modes associated with Zn2+ coordination.
  • Quantum chemical calculations were performed to support spectral interpretations and model the coordination structure.

Main Results:

  • ATR-FTIR spectra revealed characteristic IR features corresponding to histidine (C5-N1) and carboxylate (COO-) stretches, as well as changes in amide I bands indicative of alterations in α-helical structures.
  • Vibrational frequency analysis suggested that Zn2+ is coordinated in a monodentate fashion by an anionic carboxylate group and by the N1 (Nτ) position of a neutral imidazole ring of histidine.
  • The results indicate a tetrahedral coordination geometry involving carboxylate, imidazole groups, and a water molecule.

Conclusions:

  • Zn2+ binds to the extracellular domain of Hv1/VSOP through coordination with histidine and carboxylate residues.
  • The binding involves a specific coordination mode and geometry, leading to inhibition of channel activity.
  • This study provides a detailed molecular understanding of Zn2+ interaction with Hv1/VSOP, crucial for its physiological and pathological roles.