Abstract
During glycine oxidation by spinach leaf mitochondria, oxygen consumption showed a strong and transient inhibition upon addition of oxaloacetate or aspartate plus α-ketoglutarate. During the course of the inhibition, aspartate and α-ketoglutarate were stoichiometrically transformed into malate and glutamate.
It is concluded that oxaloacetate formed by transamination is reduced by the malate dehydrogenase, which allows the regeneration of NAD+ for glycine oxidation and, thus, by-passes the respiratory chain. Efficiency of a malate-glutamate/aspartate-α-ketoglutarate shuttle upon illumination and under in vivo conditions is discussed.
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Selected References
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