Key result
Zn2+ binding to the voltage-gated proton channel Hv1/VSOP likely involves a tetrahedral coordination structure with carboxylate and imidazole groups and a water molecule.
This basic science study elucidates the tetrahedral coordination structure of Zn2+ binding to the voltage-gated proton channel Hv1/VSOP.
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Elucidates Zn2+ coordination in Hv1/VSOP; hypothesis-generating for human channel modulation.
The voltage-gated proton channel (Hv1/VSOP) is inhibited by Zn 2+, of which the binding site is located in the extracellular region. We utilized attenuated total reflection–Fourier transform infrared (ATR-FTIR) spectroscopy to examine the coordination structure by monitoring protein structural changes induced by Zn 2+ -binding. The Zn 2+ -induced difference ATR-FTIR spectra of Hv1 showed IR features that can be assigned to the histidine C5–N1 and carboxylate-COO – stretches as well as amide I changes likely in α-helical peptide bonds. Analysis of vibrational frequencies indicated that the Zn 2+ is coordinated by the anionic carboxylate with monodentate mode and by the histidine at N1 (Nτ) position of the neutral imidazole form. Combined with quantum chemical calculations, the most probable coordination structure was proposed as a tetrahedral geometry with ligands of carboxylate and imidazole groups in addition to a water molecule.
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Iwaki et al. (2018) studied this question. Zn2+ binding was evaluated on Coordination structure of Zn2+ binding site. Zn2+ binding to the voltage-gated proton channel Hv1/VSOP likely involves a tetrahedral coordination structure with carboxylate and imidazole groups and a water molecule.
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