Mitochondrial oxygen affinity as a function of redox and phosphate potenitals

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Abstract

1. The conditions under which mitochondria might catalyse a net reversal of oxidative phosphorylation are analysed. 2. Rat-liver mitochondria, incubated under such conditions, show a strongly diminished affinity for oxygen. 3. The velocity of respiration under these conditions is a hyperbolic function of the oxygen concentration. 4. The Kmfor oxygen is less than 0.1 μM at low phosphate potential, irrespective of substrate, and 1-3 μM under reversal conditions. 5. The observed kinetics can be accounted for in a simple mechanism for cytochrome oxidase action. © 1975.

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Bienfait, H. F., Jacobs, J. M. C., & Slater, E. C. (1975). Mitochondrial oxygen affinity as a function of redox and phosphate potenitals. BBA - Bioenergetics, 376(3), 446–457. https://doi.org/10.1016/0005-2728(75)90166-8

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