Abstract
1. The breakdown of pyruvate was examined in whole cells and cell-free extracts of the blue-green alga Anabaena variabilis. Decarboxylation of specifically labelled pyruvate indicated a similar metabolic route to that of acetate, although no pyruvate oxidase was present. Pyruvate: ferredoxin oxidoreductase was detected in cell-free extracts and after DEAE-cellulose treatment, addition of ferredoxin was necessary for pyruvate decarboxylation; acetyl-CoA was the first product of the reaction. 2. The formation of acetyl-CoA from pyruvate required ATP; kinetic evidence as well as experiments with [ γ- 32P]ATP indicated that this serves as an activator and not as a substrate in the reaction. The importance of this reaction in the control of biosynthesis and nitrogen fixation is discussed.
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