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- W4381108210 abstract "It is shown that the functioning of ATP synthase factor F1, on which the reaction of adenosine triphosphate (ATP) synthesis takes place, involves hydrogen ions that enter F1 after transmembrane transfer through the FO subunit. The protonation of amino-acid residues of glutamate and aspartate significantly changes the conformation of the enzyme, which is an important factor facilitating conformational transitions in ATP synthase along with mechanical movement of the γ subunit described in publications. The binding of protons to ATP synthase factor F1 during enzyme functioning is also necessary to ensure the ATP synthesis reaction itself, which does not slow down under nonequilibrium conditions of alkalization of the near-membrane zone during the functioning of proton pumps thanks to the use of protons transmembranely transferred through FO. The rotation of ATP synthase in this case can catalyze the exchange of protons between the phases of near-membrane and bulk water. It is concluded that the conformational model of ATP synthase should be supplemented and it should take into account protonation of the F1 factor." @default.
- W4381108210 created "2023-06-18" @default.
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- W4381108210 date "2023-02-01" @default.
- W4381108210 modified "2023-10-15" @default.
- W4381108210 title "On the Role of Protons in the Functioning of ATP Synthase Factor F1 during Adenosine-Triphosphate Synthesis" @default.
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- W4381108210 doi "https://doi.org/10.1134/s263516762301007x" @default.
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