Abstract

FOF1-ATP synthase is a highly conserved enzyme of eukaryotic or bacterial cells. This enzyme contains eight species of various subunits in bacteria. The F1 sector contains subunits α₃, β₃, γ, δ, and ε, and the FO sector contains subunits a, b₂, and c_(10–15). According to modern nomenclature, the rotor of FOF1-ATF synthase consists of the γ, ε, and c subunits; the stator of the enzyme molecule includes the α₃, β₃, δ, a, and b₂ subunits. The rotation of the complex relative to the stator subunits leads to the synthesis or hydrolysis of ATP with the translocation of protons through the a subunit and c ring of the FO sector. The most famous ATP synthase inhibitor is oligomycin A. Oligomycin A inhibits proton translocation in the FOF1-ATP synthase complexes, which leads to an impaired energy metabolism in cells. Oligomycin has a cytotoxic effect against a number of pathogenic bacteria and a high antitumor activity due to the inactivation of FOF1-ATF synthase, a promising biological target for modern drugs. Since FOF1-ATP synthase is highly conserved and ATP synthesis is one of the central processes necessary for the vital functions of cells, this enzyme is a promising biotarget for new antibacterial drugs synthesized based on oligomycin A. This article describes the latest data on the functioning of ATP synthase in bacterial and eukaryotic cells, as well as recent work on the development of new antibacterial drugs based on oligomycin A and its derivatives.

中文翻译：

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细菌FOF1 ATP：用于ATP合成和水解的纳米马达，以及与大环内酯类抗生素寡霉素A相互作用的机理

摘要

FOF1-ATP合酶是真核或细菌细胞的高度保守的酶。该酶在细菌中包含八种不同的亚基。F1的扇区包含亚基α ₃，β ₃，γ，δ，ε和FO扇区包含亚基A，B ₂，和c _（10-15） 。根据现代命名法，FOF1-ATF合酶的转子由γ，ε和c亚基组成。酶分子的定子包括α ₃，β ₃，δ，a和b ₂亚单位。复合物相对于定子亚基的旋转导致ATP的合成或水解，质子通过FO区段的a亚基和c环移位。最著名的ATP合酶抑制剂是寡霉素A。寡霉素A抑制FOF1-ATP合酶复合物中的质子移位，从而导致细胞能量代谢受损。由于FOF1-ATF合酶（现代药物的有希望的生物学靶标）的失活，寡霉素对多种病原菌具有细胞毒性作用，并具有很高的抗肿瘤活性。由于FOF1-ATP合酶是高度保守的并且ATP合成是细胞重要功能所必需的主要过程之一，因此该酶是基于寡霉素A合成的新型抗菌药物的有希望的生物靶标。