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Mitochondrial cytochrome oxidase is competitively and reversibly inhibited by inhibitors that bind to ferrous heme, such as carbon monoxide and nitric oxide. In the case of nitric oxide, nanomolar levels inhibit cytochrome oxidase by competing with oxygen at the enzyme's heme-copper active site. This raises the K m for cellular respiration into the physiological range. This effect is readily...
The kinetics of the inhibition of mitochondrial respiration by NO was examined in isolated mitochondria (here obtained from rat brown adipose tissue). The K i of NO for the inhibition was ∼27 nM; the IC 50 of NO increased in proportion to the square of an increase in O 2 tension. The K m of O 2 for respiration was ∼16 μM; in the presence of NO, the dependence...
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