The pyruvate: ferredoxin oxidoreductase in heterocysts of the cyanobacterium Anabaena cylindrica.
Heterocyst preparations have been obtained which actively perform nitrogen fixation (C2H2 reduction) and contain the enzymes of glycolysis and some of the tricarboxylic acid cycle. Pyruvate: ferredoxin oxidoreductase has been unambiguously demonstrated in extracts from heterocysts by the formation of acetylcoenzyme A, CO2 and reduced methyl viologen (ferredoxin) from pyruvate, coenzyme A and oxidized methyl viologen (ferredoxin) as well as by the synthesis of pyruvate from CO2, acetylcoenzyme A and reduced methyl viologen. Pyruvate supports C2H2 reduction by isolated heterocysts, however, with lower activity than Na2S2O4 and H2. alpha-Ketoglutarate: ferredoxin oxidoreductase is absent in Anabaena cylindrica, confirming that the organism has an incomplete tricarboxylic acid cycle.
D002250:Carbon Radioisotopes; D000458:Cyanobacteria / Q000201:enzymology*; D006019:Glycolysis; D007658:Ketone Oxidoreductases / Q000378:metabolism*; D007700:Kinetics; D050743:Pyruvate Synthase; D011773:Pyruvates / Q000378:metabolism; D019289:Pyruvic Acid; D013172:Spores, Fungal / Q000201:enzymology*
D002250:Carbon Radioisotopes; D011773:Pyruvates; D019289:Pyruvic Acid; D007658:Ketone Oxidoreductases; D050743:Pyruvate Synthase