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• W3022755754 abstract "Dysfunction of mitochondrial enzymes, including ATP synthase, has been implicated in type-2 diabetes, cancer, heart disease, and neurodegenerative diseases. Our electric field driven torque (EFT) model of ATP synthase predicts a scaling law relating torque to the number of proton binding sites in the rotor (c-ring) and the proton motive force (pmf) across the mitochondrial inner membrane. When the FO complex of ATP synthase is coupled to F1, the model predicts a critical pmf to drive ATP production. In order to fully understand how the electric field resulting from the pmf drives the c-ring to rotate, it is also important to examine the charge distribution on the protonated c-ring and in the a-subunit, which contains the proton half-channels and acts as a stator. A self-consistent field approach is used in our calculations, based on a refinement of reported ac12 structural data. The calculations reveal changes in pKa for key residues on the a-subunit and c-ring, as well as titration curves and protonation state energy diagrams. Implications for the EFT model will be discussed. Support was provided by R21CA133153 from NHLBI and NCI at NIH and from NSF, and by grant E-1221 from the R. A. Welch Foundation. Additional support was provided by the State of Texas through the Texas Center for Superconductivity and the Norman Hackerman Advanced Research Program." @default.
• W3022755754 created "2020-05-13" @default.
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• W3022755754 date "2010-01-01" @default.
• W3022755754 modified "2023-09-28" @default.
• W3022755754 title "Electric Field Driven Torque in ATP Synthase" @default.
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• W3022755754 doi "https://doi.org/10.1016/j.bpj.2009.12.4025" @default.
• W3022755754 hasPublicationYear "2010" @default.
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