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- W2037221520 abstract "Free energy changes for ATP synthesis (delta GP) and 2e(-)-transfer across Site 3 (delta GR) were determined during oxidative phosphorylation by rat liver mitochondria. At static head, -delta GR/delta GP ranged narrowly between 1.55 and 1.59 with five different respiratory substrates. Thus, an ATP/2e- of 1 1/2 at Site 3 is thermodynamically possible with regards to overall reactants and products. Using nonequilibrium thermodynamics, phenomenological stoichiometries were close to 1 1/2 for all substrates suggesting that ATP/2e- at Site 3 is, in fact, 1 1/2. An ATP/2e- of 1 1/2 can only be possible if H+/O is 4 for cytochrome oxidase." @default.
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- W2037221520 date "1987-01-01" @default.
- W2037221520 modified "2023-09-25" @default.
- W2037221520 title "An ATP2e− stoichiometry of 112 is thermodynamically possible for Site 3 of oxidative phosphorylation" @default.
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- W2037221520 doi "https://doi.org/10.1016/0006-291x(87)90467-0" @default.
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