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- W2077802255 abstract "Particles separated from extracts of tobacco leaves by differential centrifugation catalysed the conversion of two molecules of glycine to one molecule of serine and one of carbon dioxide. The catalytic system was inhibited by inhibitors of the mitochondrial electron transport system. The reaction was slow in the absence of oxygen but attained a maximum rate at 3% by vol. of oxygen in the atmosphere. Approximately one atom of oxygen was taken up for each molecule of serine formed. Added ADP increased the rate of reaction and was converted to ATP. Some ATP was formed and oxygen consumed in the absence of glycine but both processes proceeded faster when glycine was added. Isonicotinyl hydrazide, an inhibitor of serine synthesis, decreased phosphorylation more in the presence of glycine than in its absence. Trans-aconitate, a competitive inhibitor of aconitase, did not inhibit the phosphorylation caused by adding glycine but strongly inhibited phosphorylation occuring in the absence of glycine. Phosphorylation accompanying the conversion of glycine to serine probably involves the electron transport chain of mitochondria and associated phosphorylation sites. The conversion of glycine to serine is probably responsible for the evolution of carbon dioxide in photorespiration, so our results suggest that photorespiration causes ATP to be synthesized in mitochondria during photosynthesis." @default.
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- W2077802255 title "Oxidation and phosphorylation associated with the conversion of glycine to serine" @default.
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