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Исследование роли С-концевого регуляторного домена субъединицы эпсилон в FoF1-АТФ-синтазе Bacillus subtilisкурсовая работа (Специалист)
- Научные руководители: Лапашина А.С., Фенюк Б.А.
- Автор: Зубарева Валерия Михайловна
- Тип: Специалист
- Организация, в которой проходила защита: МГУ имени М.В. Ломоносова
- Кафедра: Факультет биоинженерии и биоинформатики
- Год защиты: 2020
- Курс: 2
- Аннотация: F OF1-ATP synthase is a membrane enzyme which catalyzes ATP synthesis using the energy of transmembrane electrochemical proton gradient. The enzyme may function in a reverse mode as ATP-dependent proton pump. F OF1-ATP synthase consists of two parts: water-soluble F1 catalyzing ATP synthesis or hydrolysis, and membrane Fo performing transmembrane proton transport. Bacterial F 1 consists of 𝛼3𝛽3 hexamer carrying 3 catalytic and 3 noncatalytic sites, and subunits 𝛾, 𝛿, and 𝜀. Bacterial FO subcomplex contains 8-15 copies of c subunit arranged in a ring-shaped structure, one copy of a subunit and two b subunits. A subcomplex of 𝛾𝜀c8-15 rotates with respect to 𝛼3𝛽3ab2𝛿 subcomplex when protons are being transported across the membrane. This process is coupled with conformational transitions in catalytic sites. The ATPase activity of ATP synthase is suppressed by MgADP complex in an uncompetitive manner - a phenomenon known as MgADP inhibition. When ADP is bound in the catalytic site in absence of inorganic Pi, the enzyme may lapse into inactive state. In chloroplasts and some bacteria, ATP hydrolysis may also be suppressed by C-terminal domain of 𝜀 subunit [1]. Among bacteria, the inhibitory effect of 𝜀 have been observed in Escherichia coli, Bacillus sp. PS3 and Bacillus subtilis [2-6]. Relationship between MgADP inhibition and 𝜀-dependent inhibition is obscure. Some authors have claimed that 𝜀 subunit relieves ATP synthase from MgADP inhibition and activates the enzyme [6]. Others have demonstrated that both types of inhibition support each other [7]
- Добавил в систему: Фенюк Борис Александрович