Abstract
Extracts from the nitrogen fixing blue-green algaAnabaena cylindrica catalyse a pyruvate decarboxylation, which is dependent on ferredoxin and stimulated by coenzyme A, ATP and a SH-protecting compound. This pyruvate clastic reaction is completely reversible: The net synthesis of pyruvate requires CO2, acetyl-coenzyme A and reduced ferredoxin. Preparations fromAnabaena cylindrica also catalyse the exchange reaction between CO2 and the carboxyl group of pyruvate. Thus the enzyme fromAnabaena cylindrica has essentially all the characteristics known for the pyruvate: ferredoxin oxidoreductase from anaerobic bacteria.
The activity of the pyruvate: ferredoxin oxidoreductase inAnabaena grown with ammonia is lower than one-fifth of that in cells grown with molecular nitrogen or nitrate as the nitrogen source. From this, it will be concluded that a physiological role of the reaction is to generate reduced ferredoxin for the assimilation of nitrogen to ammonia. The pyruvate synthesis is probably not physiological inA. cylindrica.
In addition, extracts fromA. cylindrica also catalyse a ferredoxin dependent decarboxylation of α-ketoglutarate. It is not yet clear, whether this ketoglutarate cleavage has a function inA. cylindrica.
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Bothe, H., Falkenberg, B. & Nolteernsting, U. Properties and function of the pyruvate: Ferredoxin oxidoreductase from the blue-green algaAnabaena cylindrica . Arch. Microbiol. 96, 291–304 (1974). https://doi.org/10.1007/BF00590185
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DOI: https://doi.org/10.1007/BF00590185