Regulation of the NADH and NADPH-ferredoxin oxidoreductases in Clostridia of the butyric group

摘要: NADH and NADPH-ferredoxin oxidoreducatases have been studied in Clostridium acetobutylicum, Cl. tyrobutyricum pasteurianum. The study of the distribution regulation these enzymatic activities well-defined culture conditions, reveals that essential function oxidoreductase is to produce NADPH, while NADH-ferredoxin can, depending on cellular or oxidize NADH. When Clostridia use glycolysis, by acetyl-CoA (obligatory activator reductase activity) (competitive inhibitor ferredoxin-NAD+ allow enzymes correlatively with glyceraldehyde-3-phosphate dehydrogenase thus control levels NAD+ cell. In pasteurianum, ferredoxin-NADP+ activity are regulated accordance intracellular concentrations coenzymes. In growing pyruvate/acetate, cannot be detected; only found. this Clostridium, ferrodoxin-NADP+ same whether it grown glucose pyruvate. Contrary this, undergoes a drastic change, since no longer controls activity. case necessary, does not function.