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- W2102213108 abstract "The oxygen dependence of mitochondrial oxidative phosphorylation was measured in suspensions of isolated rat liver mitochondria using recently developed methods for measuring oxygen and cytochrome c reduction. Cytochrome- c oxidase (energy conservation site 3) activity of the mitochondrial respiratory chain was measured using an artificial electron donor ( N, N, N′, N′-tetramethyl- p-phenylenediamine) and ascorbate to directly reduce the cytochrome c, bypassing sites 1 and 2. For mitochondrial suspensions with added ATP, metabolic conditions approximating those in intact cells and decreasing oxygen pressure both increased reduction of cytochrome c and decreased respiratory rate. The kinetic parameters [ K M and maximal rate ( V M )] for oxygen were determined from the respiratory rates calculated for 100% reduction of cytochrome c. At 22°C, the K M for oxygen is near 3 Torr (5 μM), 12 Torr (22 μM), and 18 Torr (32 μM) at pH 6.9, 7.4, and 7.9, respectively, and V M corresponds to a turnover number for cytochrome c at 100% reduction of near 80/s and is independent of pH. Uncoupling oxidative phosphorylation increased the respiratory rate at saturating oxygen pressures by twofold and decreased the K M for oxygen to <2 Torr at all tested pH values. Mitochondrial oxidative phosphorylation is an important oxygen sensor for regulation of metabolism, nutrient delivery to tissues, and cardiopulmonary function. The decrease in K M for oxygen with acidification of the cellular environment impacts many tissue functions and may give transformed cells a significant survival advantage over normal cells at low-pH, oxygen-limited environment in growing tumors." @default.
- W2102213108 created "2016-06-24" @default.
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- W2102213108 date "2012-12-15" @default.
- W2102213108 modified "2023-10-17" @default.
- W2102213108 title "Oxygen, pH, and mitochondrial oxidative phosphorylation" @default.
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- W2102213108 doi "https://doi.org/10.1152/japplphysiol.01160.2012" @default.
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