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Acid-treated extracts ofEscherichia coli were tested for their ability to restore reduced nicotinamide adenine dinucleotide phosphate-nitrate reductase activity to an extract of aNeurospora nit-1 mutant which produces a defective enzyme. With wild-typeE. coli this complementation activity was more readily detected in the cytoplasmic fraction, although the nitrate reductase activity was found primarily in the particulate fraction.chlB mutants ofE. coli appeared to have more complementation activity in the cytoplasm than was observed in the wild type, but no activity in the particulate fraction. The otherchl mutants had little or no activity in either fraction. These results suggest thatchlB mutants can produce a component or cofactor which is missing in the other mutants and in theNeurospora mutant, but cannot transfer it to the nitrate reductase enzyme.

journal of bacteriology

Restoration of Reduced Nicotinamide Adenine Dinucleotide Phosphate-Nitrate Reductase Activity of a <i>Neurospora</i> Mutant by Extracts of Various Chlorate-Resistant Mutants of <i>Escherichia coli</i>

Restoration of Reduced Nicotinamide Adenine Dinucleotide Phosphate-Nitrate Reductase Activity of a Neurospora Mutant by Extracts of Various Chlorate-Resistant Mutants of Escherichia coli