Abstract
In mitochondrial oxidative phosphorylation, free energy is liberated to drive ATP synthesis at three coupling sites — Sites 1, 2 and 3. In keeping with chemiosmotic principles (Mitchell, 1961, 1965), each of these coupling sites generates an electrochemical gradient of protons (Δμ̃H +) across the membrane. There remains, however, considerable disagreement as to the proton stoichiometries for these sites as well as for the proton stoichiometries of the proton-translocating ATPase and the various transport systems.
This work was supported, in part, by Grants HL35490 and DK37034 from NIH. *Dr. Freedman’s current address is Department of Biology, Syracuse University, Syracuse, NY 13244.
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Lemasters, J.J., Freedman, J.A., Fleishman, K.E., Dawson, T.L. (1988). ATP/2e− Stoichiometries for the Coupling Sites of Mitochondrial Oxidative Phosphorylation: Evaluation by Equilibrium and Non-Equilibrium Thermodynamics. In: Lemasters, J.J., Hackenbrock, C.R., Thurman, R.G., Westerhoff, H.V. (eds) Integration of Mitochondrial Function. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2551-0_14
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