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- W4309775304 abstract "Previous research has suggested that molecular energy converters such as ATP synthases, ion pumps, and cotransporters operate via spatially separate pathways for free energy donor and acceptor reactions linked by a protein molecule. We present a chemical kinetics model based on these works, with the basic assumption that all molecular energy converters can be thought of as linked enzymatic reactions, one running downhill the chemical potential gradient and driving the other uphill. To develop the model we first look at how an enzyme process can be forced to go backwards using a basic kinetic model. We then use these findings to suggest a thermodynamically consistent method of linking two enzymatic reactions. Finally, in the context of the aforementioned energy converters, the thermodynamic performance of the resulting model is thoroughly investigated and the obtained results are contrasted with experimental data." @default.
- W4309775304 created "2022-11-29" @default.
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- W4309775304 date "2023-02-01" @default.
- W4309775304 modified "2023-09-30" @default.
- W4309775304 title "Thermodynamic performance of coupled enzymatic reactions: A chemical kinetics model for analyzing cotransporters, ion pumps, and ATP synthases" @default.
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- W4309775304 doi "https://doi.org/10.1016/j.bpc.2022.106932" @default.
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