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Analysis of an electrostatic mechanism for ΔpH dependent gating of the voltage-gated proton channel, HV1, supports a contribution of protons to gating chargeстатья Электронная публикация
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 29 сентября 2021 г.
- Авторы: Sokolov Valerij S., Cherny Vladimir V., Ayuyan Artem G., DeCoursey Thomas E.
- Журнал: Biochimica et Biophysica Acta - Bioenergetics
- Том: 1862
- Номер: 11
- Год издания: 2021
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Номер статьи: 148480
- DOI: 10.1016/j.bbabio.2021.148480
- Аннотация: Voltage-gated proton channels (HV1) resemble the voltage-sensing domain of other voltage-gated ion channels, but differ in containing the conduction pathway. Essential to the functions of HV1 channels in many cells and species is a unique feature called ΔpH dependent gating. The pH on both sides of the membrane strictly regulates the voltage range of channel opening, generally resulting in exclusively outward proton current. Two types of mechanisms could produce ΔpH dependent gating. The “countercharge” mechanism proposes that protons destabilize salt bridges between amino acids in the protein that stabilize specific gating configurations (closed or open). An “electrostatic” mechanism proposes that protons bound to the channel alter the electrical field sensed by the protein. Obligatory proton binding within the membrane electrical field would contribute to measured gating charge. Estimations on the basis of the electrostatic model explain ΔpH dependent gating, but quantitative modeling requires calculations of the electric field inside the protein which, in turn, requires knowledge of its structure. We conclude that both mechanisms operate and contribute to ΔpH dependent gating of HV1.
- Добавил в систему: Соколов Валерий Сергеевич