Abstract
From many studies conducted to determine the stoichiometry of mitochondrial oxidative phosphorylation employing a remarkable variety of techniques and discarding several common systematic errors, there has been an increasing consensus in recent years. In mammalian mitochondria, the measured values of ATP/2e- were close to 1, 0.5 and 1 at the three “coupling sites”, respectively1,2. However, such determinations have been made under conditions where the electron flux through each respiratory unit is maximum (State 3) even if the number of functional units is changed by using inhibitor titration.
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© 1993 Springer Science+Business Media New York
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Fitton, V., Rigoulet, M., Guérin, B. (1993). Mechanistic Stoichiometry of Yeast Mitochondrial Oxidative Phosphorylation: A Behavior of Working Engine. In: Schuster, S., Rigoulet, M., Ouhabi, R., Mazat, JP. (eds) Modern Trends in Biothermokinetics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2962-0_46
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DOI: https://doi.org/10.1007/978-1-4615-2962-0_46
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