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May 8, 2026

Synergistic actions on hHv1 proton channel gating by singlet oxygen-mediated photodynamic modification, voltage, pH, and subunit cooperativity.

Ziyü Sun Ya Li Yanlin Huang Xuanxuan Huang Jiajie Li Xiaoxi Li Qinglian Liu Lei Zhou

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Key Points

This research aims to understand how different factors influence the gating mechanisms of the hHv1 proton channel.
Examined the effects of photodynamic modification on hHv1 channel gating
Analyzed the influence of voltage and pH on channel behavior
Investigated subunit cooperativity in dimeric assembly of the channel.
Photodynamic modification significantly alters the gating of the hHv1 channel.
Voltage and pH variations affect channel behavior, indicating a complex interplay in gating mechanisms.
Subunit cooperativity plays a crucial role in the functioning of the hHv1 proton channel.

Implication

Investigates factors influencing hHv1 channel gating, suggesting new modulation strategies.

Abstract

The human Hv1 (hHv1) channel adopts a dimeric assembly, and each protomer shares homology with the voltage-sensing domain of voltage-gated K

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Cite This Study

Sun et al. (2026) studied this question.

synapsesocial.com/papers/6a02c364ce8c8c81e9640ba6 https://doi.org/10.1016/j.bpj.2026.05.012

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Keep reading

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1Singlet oxygen modification abolishes voltage-dependent inactivation of the sea urchin spHCN channelOriginal Research · 2018 · 8 citations
2Dimer interaction in the Hv1 proton channelpreclinical · 2020 · 27 citations
3Activation pathway of the human voltage-gated proton channelOriginal Research · 2026
4Opening of rod photoreceptor CNG channels by photodynamically generated singlet oxygenOriginal Research · 2026 · 1 citations
5Interrogation of the intersubunit interface of the open Hv1 proton channel with a probe of allosteric couplingpreclinical · 2015 · 26 citations

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